U.S. International Trade Commission

In the Matter of

Publication 4113 November 2009

Washington, DC 20436

Investigation No. 337-TA-571

Certain L-Lysine Feed Products, Their 

Methods Of Production And Genetic 

Constructs For Production 
U.S. International Trade Commission

Address all communications to 

Secretary to the Commission 

United States International Trade Commission 

Washington, DC 20436

COMMISSIONERS 

Shara L. Aranoff, Chairman 

Daniel R. Pearson, Vice Chairman 

Deanna Tanner Okun 

Charlotte R. Lane 

Irving A. Williamson 

Dean A. Pinkert 
U.S. International Trade Commission

Washington, DC 20436 

www.usitc.gov

In the Matter of

Publication 4113 November 2009

Investigation No. 337-TA-571

Certain L-Lysine Feed Products, Their 

Methods Of Production And Genetic 

Constructs For Production 


sale within the United States after importation of certain L-lysine feed products and genetic 

constructs for production thereof by reason of infi-ingement of claims 13, 15-1 9, and 2 1-22 of 

U.S. Patent No. 5,827,698 (“the ‘698 patent”) and claims 1,2, 15, and 22 of U.S. Patent No. 

6,040, 160 (“the ‘ 160 patent”). 

The complaint named as respondents Global Bio-Chem Technology, Group Company 

Ltd. (Admiralty, Hong Kong), Changchun Dacheng Bio-Chem Engineering Development Co., 

Ltd., (Jilin Province, China), Changchun Baocheng Bio Development Co., Ltd. (Jilin Province, 

China), Changchun Dahe Bio Technology Development Co., Ltd. (Jilin Province, China), BioChem Technology (HK) Ltd. (Admiralty, Hong Kong) (collectively, “GBT”). 7 1 Fed. Reg. 

30958. On June 29,2006, Ajinomoto Heartland further amended the complaint and notice of 

institution by adding its parent company, Ajinomoto, Inc. (Tokyo, Japan) as a complainant. 71 

Fed. Reg. 43209 (July 3 1,2006). 

On October 15,2007, the Commission determined not to review an order of the ALJ, 

granting Ajinomoto’s motion to withdraw claims 1, 2, and 22 of the ‘160 patent and claims 13, 

16-19, and 21 -22 of the ‘698 patent. 

On July 3 1,2008, the ALJ issued his final ID, in which he found no violation of section 

337 with regard to either the ‘160 or the ‘698 patents because he found that the asserted claims of 

both patents were invalid for failure to satisfy the best mode requirement of 35 U.S.C. 9 112 T[ 1 

on two separate grounds and that both patents were unenforceable because of inequitable 

conduct. He found infringement of the asserted claims through importation of lysine made using 

the “old” strain of E. coli by GBT, but not the “new” strain, based upon the stipulation of the 

parties. The ALJ also found the existence of a domestic industry for the asserted claims, and 

found that the asserted claims were not invalid for obviousness or obviousness-type double 

patenting, and that the asserted patents were not unenforceable by reason of unclean hands. 

On August 19,2008, Ajinomoto petitioned for review of the ALJ’s final ID regarding 

invalidity of the asserted claims for failure to meet the best mode requirement and 

unenforceability of the patents because of inequitable conduct. Neither GBT nor the 

Commission investigative attorney petitioned for review of any part of the ID. 

Having examined the relevant portions of the record in this investigation, including the 

final ID, the petition for review, and the responses thereto, the Commission has determined (1) to 

review and take no position on (a) the ALJ’s finding that claim 15 of the ‘ 160 patent is invalid 

for failure to meet the best mode requirement to the extent that finding is based on alleged 

fictitious data and (b) the ALJ’s finding that the ‘ 160 patent is unenforceable for inequitable 

conduct and (2) not to review the remainder of the ID. Thus, the investigation is terminated with 

a finding of no violation of section 337. 

2 
This action is taken under the authority of section 337 of the Tariff Act of 1930, as 

amended (19 U.S.C. 0 1337), and in sections 210.42 - .46 of the Commission’s Rules of Practice 

and Procedure (19 C.F.R. 5s 210.42 - .46). 

By order of the Commission. - 

Marilyn R. Abbow 

Secretary to the Commission 

Issued: September 29,2008 

3 
CERTAIN L-LYSINE FEED PRODUCTS, THEIR METHODS 337-TA-571 

OF PRODUCTION AND GENETIC CONSTRUCTS FOR 

PRODUCTION 

PUBLIC CERTIFICATE OF SERVICE 

I, Marilyn R. Abbott, hereby certify that the attached NOTICE OF COMMISSION 

DETERMINATION (1) TO REVIEW AND NOT TAKE A POSITION ON 

CERTAIN ISSUES IN THE FINAL INITIAL DETERMINATION OF THE 

ADMINISTRATIVE LAW JUDGE AND (2) NOT TO REVIEW THE 

REMAINDER OF THE FINAL INITIAL DETERMINATION; TERMINATION 

OF THE INVESTIGATION has been served by hand upon the Commission 

Investigative Attorney Juan S. Cockbum, Esq., and the following parties as indicated, on 

r 79. 3008 

US. International Trade Commission 

500 E Street, SW 

Washington, DC 20436 

ON BEHALF OF COMPLAINANT AJINOMOTO 

HEARTLAND LLC AND AJINOMOTO, INC.: 

Frank R. Samolis, Esq. 

PATTON BOGGS LLP 

2550 M Street, NW 

Washington, DC 20037 

P-202-457-6000 

ON BEHALF OF RESPONDENTS GLOBAL BIOCHEM TECHNOLOGY GROUP COMPANY 

ENGINEERING DEVELOPMENT CO., LTD., 

DEVELOPMENT CO., LTD., CHANGCHUN DAHE 

BIO TECHNOLOGY DEVELOPMENT CO., LTD., 

LIMITED, CHANGCHUN DACHENG BIO-CHEM 

CHANGCHUN BAOCHENG BIO-CHEM 

AND BIO-CHEM TECHNOLOGY LIMITED: 

( ) Via Hand Delivery 

( ) Via Overnight Mail 

(9 Via First Class Mail 

( )Other: 

Tom M. Schaumberg, Esq. 

ADDUCI, MASTRIANI & SCHAUMBERG LLP 

1200 Seventeenth Street, NW 

Fifth Floor ( ) Other: 

Washington, DC 20036 

( ) Via Hand Delivery 

( ) Via Overnight Mail 

Q Via First Class Mail 
Page 2 - Certificate of Service 

P-202-467-6300 

F-202-466-2006 


Ruixue Ran, Esq.; of East Associates fiom Beijing, China 

For the Commission Investiaative Staff 

Lynn I. Levine, Esq., Director; Anne Goalwin, Esq., Supervising Attorney; Juan Cochburn, Esq., 

Investigative Attorney; of the Office of Unfair Import Investigations, U.S. International Trade 

Commission, from Washington, D.C. 
TABLE OF CONTENTS 

DISCUSSION ................................................................ 2 

I . Introduction ........................................................... 2 

A . ProceduralHisto ry ................................................ 2 

B . The Parties ...................................................... 4 

1 . Complainant ............................................... 4 

2 . Respondents ............................................... 5 

C . Overview of the Technology ........................................ 5 

D . ThePatentsatIssue ............................................... 8 

1 . U.S. Patent No . 6.040. 160 .................................... 8 

2 . U.S. Patent No . 5.827. 698 .................................... 9 

E . The Products at Issue ............................................. 11 

I1 . Jurisdiction and Importation ............................................ 11 

A . Subject Matter Jurisdiction ....................................... 12 

B . Personal Jurisdiction ............................................. 12 

I11 . RelevantLaw ......................................................... 13 

A . Validity ........................................................ 13 

1 . 13 

2 . 

3 . 

Anticipation. 35 U.S.C. 00 102 (a). (b) and (e) ................... 

Obviousness. 35 U.S.C. 3 103 (a) ............................. 15 

Written DescriptionlEnablement. 35 U.S.C. 8 112. 7 1 ........... 18 

4 . Best Mode. 35 U.S.C. 0 112. 7 1 .............................. 19 

B . Inequitable Conduct ............................................. 21 

iii 
C . UncleanHands .................................................. 23 

IV . The'160Patent ....................................................... 23 

A .............................................. . Claim Construction 23 

1 . AssertedClaims ........................................... 23 

2 . Disputed Claim Limitations ................................. 25 

B . Infringement .................................................... 25 

C . Domestic Industry . Technical Prong ................................ 26 

D . Validity ........................................................ 26 

1 . 

2 . Best Mode ................................................ 27 

3 . Obviousness .............................................. 68 

4 . 

Ordinary Skill in the Art .................................... 26 

Obviousness Double-Patenting ............................... 79 

E . Unenforceability . Inequitable Conduct ............................. 84 

V . The'698Patent ....................................................... 92 

Claim Construction .............................................. 92 

1 . 

2 . 

A . 

Asserted Claims ........................................... 92 

Disputed Claim Limitations ................................. 93 

B . Infringement .................................................... 94 

Domestic Industry . Technical Prong ................................ 94 

D . Validity ........................................................ 95 

Ordinary Skill in the Art .................................... 95 

C . 

1 . 

2 . Best Mode ................................................ 95 

iv 
3 . Obviousness ............................................. 119 

E . Unenforceability . Inequitable Conduct ............................ 129 

VI . UncleanHands ....................................................... 133 

VI1 . Domestic Industry . Economic Prong .................................... 143 

CONCLUSIONSOFLAW ................................................... 145 

INITIALDETERMINATION ................................................ 147 

RECOMMENDED DETERMINATION ON REMEDY AND BOND ............... 148 

VI11 . Remedy and Bonding .................................................. 148 

A . Limited Exclusion Order ......................................... 148 

B . Cease and Desist Order .......................................... 149 

C . Bond During Presidential Review Period ........................... 149 

APPENDIX OF EXHIBIT LISTS .............................................. A1 

V 
LIST OF ABBREVIATIONS 

CIB 

CORFF 

COSFF 

CPX 

CDX I Complainants’ demonstrative exhibit 

Complainants’ initial post-hearing brief 

Complainants’ objections to Respondents’ proposed findings of fact 

Complainants’ objections to Staffs proposed findings of fact 

Complainants’ physical exhibit 

CFF I Complainants’ proposed findings of fact 

CRB 

cx 

DeP 

Complainants’ reply post-hearing brief 

Complainants’ exhibit 

Deposition 

RIB 

Jx I Joint Exhibit 

Respondents’ initial post-hearing brief 

RDX I Respondents’ demonstrative exhibit 

SIB 

SOCFF 

SORFF 

SRB 

Tr. 

RFF 

Staffs initial post-hearing brief 

Staffs objections to Complainants’ proposed findings of fact 

Staffs objections to Respondents’ proposed findings of fact 

Staffs reply post-hearing brief 

Transcrbt 

Respondents’ proposed findings of fact 

ROCFF 

ROSFF 

RPX 

RRB 

Rx 

SFF 

~ 

Respondents’ objections to Complainants’ proposed findings of fact 

Respondents’ objections to Staffs proposed findings of fact 

Respondents’ physical exhibit 

Respondents’ reply post-hearing brief 

Respondents’ exhibit 

Staffs proposed findings of fact 

vi 
CONTAINS CONFIDENTIAL BUSINESS INFORMATION 

UNITED STATES INTERNATIONAL TRADE COMMISSION 

Washington, D.C. 

In the Matter of 

CERTAIN L-LYSINE FEED PRODUCTS, THEIR 

METHODS OF PRODUCTION AND GENETIC 

CONSTRUCTS FOR PRODUCTION 

Inv. No. 337-TA-571 

INITIAL DETERMINATION ON VIOLATION OF SECTION 337 AND 

RECOMMENDED DETERMINATION ON REMEDY AND BOND 

Administrative Law Judge Charles E. Bullock 

(July 3 1,2008) 

Pursuant to the Notice of Investigation and Rule 210.42(a) of the Rules of Practice and 

Procedure of the United States International Trade Commission, this is the Administrative Law 

Judge’s Initial Determination in the matter of certain L-lysine feed products, their methods of 

production and genetic constructs for production, Investigation No. 337-TA-57 1. 

The Administrative Law Judge hereby determines that a violation of Section 337 of the Tariff 

Act of 1930, as amended, has not been found in the importation into the United States, the sale for 

importation, or the sale within the United States after importation of certain L-lysine feed products 

in connection with claim 15 of U.S. Patent No. 6,040,160 and claim 15 of U.S. Patent No. 5,827,698. 

Furthermore, the Administrative Law Judge hereby determines that a domestic industry in the United 

States exists that practices U.S. Patent Nos. 6,040,160 and 5,827,698. 
DISCUSSION 

I. Introduction 

A. Procedural History 

This investigation was instituted by the Commission on May 24, 2006 and the notice of 

investigation was published in the Federal Regiscter on May 3 1, 2006.’ The Administrative Law 

Judge set a twelve-month target date of May 3 1, 2007 for completion of this investigation by the 

Commission in Order No. 2.2 

On June 29, 2006, Complainant Ajinomoto Heartland LLC filed a motion to amend the 

complaint to add its parent company, Ajinomoto Co., Inc. as a complainant, which was granted by 

initial determination in Order No. 5, issued on July 1 1,2006. 

On July 7,2006, the parties filed a joint motion to extend the target date by sixty days, or until 

July 20,2007, which was granted in Order No. 7, issued on July 1 1,2006. 

On December 4,2006, Complainants and Respondents filed a motion to stay this investigation 

for a period of 90 days in order to allow the parties to conduct good faith settlement discussions, 

which was granted in Order No. 1 1, issued on December 7,2006. Since the parties failed to reach 

a settlement during the stay, on April 30, 2007, the undersigned issued Order No. 12, an initial 

determination extending the target date to twenty-six months, or July 20,2008. 

On August 9,2007, Complainants filed a motion for partial termination of the investigation 

pursuant to Commission Rule 2 10.2 1 (a)( 1). Specifically, Complainants moved to withdraw claims 

1,2, and 22 of the ‘160 patent and claim nos. 13, 16-19, and 21-22 of the ‘698 patent. That motion 

’ See 71 Fed. Reg. 30958. 

See Order No. 2 (May 31,2006). 

2 
was granted by initial determination in Order No. 17, issued on August 10, 2007.3 Accordingly, the 

only remaining asserted claims are claim 15 of the ‘ 160 patent and claim 15 of the ‘698 patent. 

On August 17,2007, Respondents filed a motion for leave to amend response to the second 

amended complaint and amended notice of investigation to include additional affirmative defenses, 

which was granted by Order No. 20, issued on September 11,2007. Based on the granting of the 

motion to include additional affirmative defenses, the order directed the parties to meet and confer 

and to propose a modified procedural schedule to the undersigned. In addition, the order noted that 

the undersigned would extend the target date by initial determination, if necessary. Having received 

the proposed modified procedural schedule, the undersigned issued Order No. 21 on September 25, 

2007, an initial determination extending the target date to twenty-nine months, or October 3 1,2008. 

On October 1 1,2007, the undersigned issued Order No. 22, modifling the procedural schedule due 

to a conflict in the undersigned’s schedule. 

On November 9,2007, Complainants filed a motion for leave to file the a Third Amended 

Complaint to allege a claim of trade secret misappropriation, which was denied by Order No. 25, 

issued on November 27,2007. 

The parties have stipulated to certain material facts.4 Particular stipulated facts that are 

relevant to this Initial Determination are cited accordingly. 

An evidentiary hearing on liability was conducted before the undersigned from March 1 1-14, 

2008. In support of its case-in-chief and rebuttal case, Ajinomoto called the following witness: 

0 James Liao 

See Commission Decision Not To Review An Initial Determination Terminating The 

See JX-190C (February 19,2008 stipulation); JX-191C (March 8,2008 stipulation). 

Investigation In Part (Aug. 29,2007). 

3 
In support of its case-in-chief and rebuttal case, Respondents called the following witnesses: 

0 Kazue Kawamura 

0 Hiroyuki Koj ima 

0 Yoshimi Kikuchi 

0 Kazuo Nakanishi 

0 Ronald L. Somerville 

0 Andrew Webb 

In addition, various deposition testimony was received into evidence in lieu of direct witness 

statements or live testimony.’ 

After the hearing, post-hearing briefs and reply briefs, together with proposed findings of fact, 

conclusions of law and rebuttals to the same, were filed on April 4, 2008 and April 11, 2008, 

respectively. 

B. TheParties 

1. Complainants 

Complainants in this investigation are Ajinomoto Heartland LLC, a United States corporation 

(“Heartland”) and Ajinomoto Co., Inc. (“Ajinomoto Japan”), a Japanese corporation (collectively 

“Ajinomoto”). Heartland is a wholly-owned subsidiary of Ajinomoto Japan. Heartland is based in 

Chicago, Illinois, and has production facilities in Eddyville, Iowa. Ajinomoto Japan has its principal 

place of business in Tokyo, Japan6 Ajinomoto Japan is a worldwide leader in the areas of amino acid 

biosynthesis and commercial prod~ction.~ 

’ See CX-25 1 C (Deposition of Dehui Wang); CX-252C (Deposition of Weigang Li); RX5 1 C (Deposition of Atsushi Sasamori); RX-52C (Deposition of Yoshinari Shiroshita); RX-53C 

(Deposition of Julian Maxwell). 

ti See Second Amended Complaint, f 2.2. 

Amended Complaint, If 2.1-2.8. 

4 
2. Respondents 

Respondents in this investigation are Global Bio-Chem Technology Group Company Limited, 

Changchun Dacheng Bio-Chem Engineering Development Co., Ltd., Changchun Baocheng BioChem Development Co., Ltd., Changchun Dahe Bio Technology Development Co., Ltd., and BioChem Technology (HK) Limited (collectively “GBT”). Global Bio-Chem Technology Group 

Company Limited (“GBT Hong Kong”), is a Cayman Islands corporation with its principal place of 

business in Hong Kong. Changchun Dacheng Bio-Chem Engineering Development Co., Ltd. 

(“Dacheng Bio-Chem”) is a Chinese company with a principal place of business in Jilin Province, 

China. Changchun Baocheng Bio-Chem Development Co., Ltd. (“Baocheng Bio-Chem”) is a 

Chinese company with a principal place of business in Jilin Province, China.’ Changchun Dahe Bio 

Technology Development Co., Ltd. (“Dahe Bio Technology”) is a Chinese company with a principal 

place of business in Jilin Province, China. Complainants assert that the packaging of the accused 

products indicates that Dahe Bio Technology is the authorized manufacturer.’ Bio-Chem Technology 

(HK) Limited (“Bio Chem Technology”) assists GBT Hong Kong in the manufacture, production and 

distribution of L-lysine. Bills of lading for the accused products denote Bio Chem Technology as a 

“shipper.”’o 

C. Overview of the Technology 

At issue in this investigation are certain L-lysine feed products, their methods of production 

and genetic constructs for production. Both the ‘160 and ‘698 patents are related to the use of 

genetically engineered Escherichia bacteria that produce L-lysine (“lysine”). Lysine is an amino acid 

’ See Amended Complaint, Ex. 3-6. 

lo Amended Complaint, f 3.2,f3.10, Ex. 3-5, 10. 

Amended Complaint, fv 3.2-3.3, Ex. 3-5. 

5 
frequently added as a necessary dietary supplement in the feed of pigs and poultry. Animals fed high 

concentrations of grass or grain lack substantial amounts of lysine in their diet, and, because these 

animals cannot produce it themselves from other nutrients, lysine must be included as a dietary 

additive or supplement. Lysine and other amino acids can be produced by fermentation, viz., by 

cultivating bacteria and collecting the desired fermentation product from the culture medium. 

Wild-type E.coli” bacteria naturally convert sugars into lysine for their own internal use 

through a known biosynthetic pathway that involves a complicated sequence of intracellular 

chemical reactions. The biosynthetic pathway of L-lysine in wild-type strains of E.coli. is shown 

below:I2 

Lysine Synthesis 

Bacterial cells that have not undergone genetic engineering are known as “wild-type” cells. 

l2 See CX-235C (Kojima WS) at 7 24. 

6 
This series of reactions regulates the synthesis of lysine such that the organism makes only enough 

for the organism’s own metabolic demands. If sufficient lysine is present to meets the organism’s 

needs, certain of the reactions necessary for the cell to produce lysine become subject to “feedback 

inhibition,” viz., the presence of the end product, lysine, inhibits the E.coli fiom producing more 

lysine. The ‘ 160 patent relates to an Escherichia bacteria with genetic mutations that desensitize the 

feedback inhibited enzymes so that they continue to catalyze the reactions necessary to produce lysine 

even when the amount of lysine needed by the cell is already available. 

Wild-type E.coli also have an intracellular mechanism to break down or degrade lysine into 

other related compounds. This occurs through the known lysine degradation pathways shown 

below: l3 

Lysine Degradation 

l3 Id. at 125. 

7 
The enzymes that decompose lysine are referred to as lysine decarboxylases. The ’698 patent is 

directed to one of the lysine decarboxylase genes, known as “ldc.” The ‘698 patent teaches that this 

gene can be mutated to eliminate or reduce the decarboxylation of lysine so that the cell will not 

destroy the surplus lysine it produces. 

D. The Patents at Issue 

1. U.S. Patent No. 6,040,160 (“the ‘160 patent”) 

The ‘ 160 patent, titled “Method of Producing L-lysine by Fermentation,” was originally filed 

on December 8, 1993 in Japan with Serial #5-308397. It was subsequently filed through the Patent 

Cooperation Treaty (“PCT”) on November 28, 1994, bearing Serial PCT/JP94/01994, and was 

published June 15, 1995 as document W095/16042.’4 The application entered the national phase in 

the United States on June 9, 1997 as Serial #08/648,010 and issued as the ‘ 160 patent on March 21, 

2000.15 The named inventors are Hiroyuki Kojima, Yuri Ogawa, Kazue Kawamura and Konosuke 

Sano.16 In their declaration, the inventors of the ‘ 160 patent attest that they are the original and sole 

inventors of the subject matter set forth in the specification of the PCT application, and claim the 

benefit of the original Japanese application filing date.I7 The patent was assigned to Ajinomoto Co., 

Inc., the current owner of the ‘160 patent.18 

l4 The inventors of the ‘ 160 patent made substantial revisions which greatly expanded the 

original Japanese application to create the PCTAJS application. For example, all of the information 

in the specification subsequent to Example 6, including Figures 10-24, was added to the PCTAJS 

application. RX-89(Webb WS) at 71 31-34; RFF 1.67 (no dispute). The added text primarily 

disclosed information concerning the “enhancement” of the dapB gene, which was not mentioned 

in the original filing. RX-89(Webb WS) at f 34; RFF 1.68-1.69 (no dispute). 

l5 See JX-1, cover page. 

l6 Id. 

l7 JX-112 at AAH LOOO595-597; CX-126. 

” See JX-l9OC at 7 2. 

8 
The Japanese priority application for the ‘ 160 patent identifies mutations in two genes in the 

biosynthesis pathway of L-lysine. One of these pathways for the production of lysine uses an enzyme, 

dihydrodipicolinate synthase (“DDPS”), which is encoded by the dapA gene. DDPS catalyzes a 

reaction in the lysine biosynthesis pathway, but can be inhibited by the presence of lysine itself 

through feedback inhibition. As previously discussed, feedback inhibition refers to a process where 

an end-product of a reaction pathway, in this case lysine, inhibits an enzyme, in this case DDPS, 

involved in the pathway to regulate the production of the end product. Thus, as the amount of lysine 

inside the cell increases, lysine binds to the DDPS enzyme, decreasing the DDPS activity and 

regulating the overall lysine production pathway. Thus, feedback inhibition hinders the production 

of lysine. 

The ‘ 160 patent has a total of 22 claims. The sole claim from the ‘ 160 patent at issue in this 

investigation is claim 15. Claim 15 covers a method of producing L-lysine by cultivating a 

microorganism of the genus Escherichia with the specified mutations in the dapA gene, producing 

and accumulating lysine in the culture and collecting the lysine from the culture.” Claim 15 is 

dependent on claim 3. Claim 3 describes the specific mutations to the dapA gene sequence at the 8 1 st 

and/or 1 18th amino acid in the DDPS enzyme.*’ 

2. U.S. Patent No. 5,827,698 (“the ‘698 patent”) 

The ‘698 patent, titled “Lysine Decarboxylase Gene and Method of Producing L-lysine,” was 

originally filed on December 9, 1994 in Japan with Serial #6- 306386.21 It was subsequently filed 

through the Patent Cooperation Treaty on December 5,1995, bearing Serial #PCT/JP95/0248 1, and 

l9 See e.g., JX-1 at 68:l-15. 

2o See id. at 6 1 :43-62: 17. 

21 See JX-2, cover page. 

9 
was published June 13,1996 as document W096/17930. The application entered the national phase 

in the United States June 9,1997, as the Serial #08/648,010 and issued as the ‘698 patent on October . 

27, 1998.22 The named inventors are Yoshimi Kikuchi, Tomoko Suzuki and Hiroyuki K~jima.~~ The 

inventors of the ‘698 patent attest that they are the original and sole inventors of the subject matter 

set forth in the specification of the PCT application, PCT/JP95/0248 1, and claim the benefits of the 

original Japanese application, Japan 6-306386, filed December 9, 1 994.24 The patent was assigned 

to Ajinomoto Co., Inc., the current owner of the ‘698 patent.25 

The ‘698 patent addresses an issue with using E. coli to produce lysine by targeting the lysine 

degradation pathway. Wild-type E.coli produce two enzymes called lysine decarboxylases that 

catalyze a reaction whereby lysine is decomposed into a by-product called cadaverine. Cadaverine 

has no nutritional value and contaminates the lysine collection process in the factory making it 

difficult and costly to separate and collect lysine from the liquid culture after removal from the 

fermentation tanks. While one gene that expresses a lysine decarboxylase, the cadA gene, was 

already known, the ‘698 patent discloses a second lysine decarboxylase gene, the ldc gene. The ‘698 

patent discloses that by eliminating the wild-type ldc gene and introducing a mutated ldc gene with 

less or no lysine decarboxylase activity, the production of the lysine decarboxylase enzyme was 

reduced or eliminated and thus, lysine degradation was eliminated. 

The ‘698 patent has a total of 22 claims. The sole claim at issue in the ‘698 patent is Claim 

15. Claim 15 of the ‘698 patent depends from claim 13, which in turn depends from claim 3 of the 

22 Id. 

23 Id. 

24 See JX-108 at AAHL000046-048. 

25 See JX-19OC T[ 1. 

10 
patent. Claim 15 covers a method of producing L-lysine using a microorganism of the species E.coli 

lacking the wild-type ldc gene, and having a mutated ldc gene to reduce or eliminate lysine 

decarboxylase expression that would otherwise degrade the lysine production.26 Claim 1 5 also covers 

the production and accumulation of lysine in a culture and collecting the lysine from the culture.27 

Claim 3 describes the specific mutations to the ldc gene.28 

E. The Products at Issue 

The product at issue is L-lysine, an amino acid, produced by genetically modified Escherichia 

bacteria. Lysine is an essential amino acid frequently added as a necessary dietary supplement in the 

feed of pigs and poultry.29 Animals fed high concentrations of grass or grain lack substantial amounts 

of lysine in their diet, and, because these animals cannot produce it themselves from other nutrients, 

lysine must be included as a dietary additive or ~upplement.~~ 

11. Jurisdiction and Importation 

Section 337 confers subject matter jurisdiction on the International Trade Commission to 

investigate, and if appropriate, to provide a remedy for, unfair acts and unfair methods of competition 

in the importation of articles into the United States. In order to have the power to decide a case, a 

court or agency must have both subject matter jurisdiction, and jurisdiction over either the parties or 

the property in~olved.~’ 

26 See JX-2 at 3 1 : 19-37. 

27 Id. 

28 Id. at 31:19-38. 

29 See JX-l9OC at 7 3; CX-231C (Liao WS) at 7 42. 

30 See CX-23 1 C (Liao WS) at 7 42. 

31 19 U.S.C. 0 1337; also see Certain Steel Rod Treating Apparatus and Components 

ThereoA Inv. No. 337-TA-97, Commission Memorandum Opinion, 21 5 U.S.P.Q. 229,23 1 (1 981) 

(“Certain Steel Rod”). 

11 
A. Subject Matter Jurisdiction 

The complaint alleges that GBT has violated Subsection 337(a)(l)(A) and (B) in the 

importation and sale ofproducts that infringe the asserted patents. Ajinomoto and GBT stipulate that 

GBT imports into the United States the accused L-lysine products, and that its products made with 

its so-called “Old E.coli” are covered by asserted claim 15 of each of the ‘ 160 and ‘698 patents.32 

Specifically, Ajinomoto and GBT stipulate that GBT has imported into the United States, and 

continues to import into the United States, L-lysine feed products manufactured using the bacteria 

strain deposited with the ATCC under Accession #SD-5590, Accession #SD-5620 and Accession 

#SD-5717.33 Ajinomoto and GBT also stipulate that after importation, such products have been sold 

to United States customers.34 Thus, the undersigned finds the Commission has jurisdiction over this 

investigation under Section 337 of the Tariff Act of 1930.35 

B. Personal Jurisdiction 

GBT has responded to the Complaint and Notice of Investigation. They have participated in 

the investigation by, among other things, participating in discovery, participating in the hearing, and 

filing pre- and post-hearing briefs. Accordingly, GBT has submitted to the personal jurisdiction of 

the Commi~sion.~~ TheCommission has in rem jurisdiction over the products at issue by virtue of 

32 See JX-190C at 779, 10, 13. 

33 JX-192C at 7 13. 

34 Id. 

35 See 19 U.S.C. 9 1337(a)(l)(A)-(B); Amgen, Inc. v. US. Int’Z Trade Comm’n, 902 F.2d 

1532, 1536 (Fed. Cir. 1990) (cLArngen”). 

36 See Certain Miniature Hacksaws, Inv. No. 337-TA-237, U.S.I.T.C. Pub. No. 1948, Initial 

Determination (unreviewed by Commission in relevant part) at 4, 1986 WL 379287 (U.S.I.T.C. 

October 15, 1986) (“Certain Miniature Hacksaws”). 

12 
GBT’s admission that the accused products have been imported into the United States.37 

111. Relevant Law 

A. Validity 

A patent is presumed valid.38 The party challenging a patent’s validity has the burden of 

overcoming this presumption by clear and convincing evidence.39 Since the claims of a patent 

measure the invention at issue, the claims must be interpreted and given the same meaning for 

purposes of both validity and infringement analyses. As with an infringement analysis, an analysis 

of invalidity involves two steps: the claim scope is first determined, and then the properly construed 

claim is compared with the prior art to determine whether the claimed invention is anticipated and/or 

rendered obvio~s.~’ 

1. Anticipation, 35 U.S.C. $3 102 (a), (b) and (e) 

A patent may be found invalid as anticipated under 35 U.S.C. 9 102(a) if “the invention was 

known or used by others in this country, or patented or described in a printed publication in this 

country, or patented or described in a printed publication in a foreign country, before the invention 

thereof by the applicant for patent.”41 A patent may be found invalid as anticipated under 35 U.S.C. 

9 102(b) if “the invention was patented or described in a printed publication in this or a foreign 

country or in public use or on sale in this country, more than one year prior to the date of the 

37 See SealedAir Corp. v. United States Int ’I Trade Comm In., 645 F.2d 976,985 (C.C.P.A. 

38 35 U.S.C. 0 282; Richardson-Vicks Inc. v. Upjohn Co., 122 F.3d 1476, 1480 (Fed. Cir. 

39 Richardson-Vicks Inc., supra; Uniroyal, Inc. v. Rudkin-Wiley Corp., 837 F.2d 1044 (Fed. 

40 Amazon.com, Inc. v. Barnesandnoble.com, Inc., 239 F.3d 1343, 1351 (Fed. Cir. 2001) 

41 35 U.S.C. 9 102(a). 

1981). 

1997) (“Richardson- Vicks”). 

Cir.) (“Uniroyal”), cert. denied, 488 U.S. 825 (1988). 

(“Amazon. com”). 

13 
application for patent in the United Under 35 U.S.C. fj 102(e), a patent is invalid as 

anticipated if “the invention was described in a patent granted on an application for patent by another 

filed in the United States before the invention thereof by the applicant for patent.”43 Anticipation is 

a question of fact.44 

Under the foregoing statutory provision, a claim is anticipated and therefore invalid when “the 

four corners of a single, prior art document describe[s] every element of the claimed invention, either 

expressly or inherently, such that a person of ordinary skill in the art could practice the invention 

without undue e~perimentation.”~~ Tobe considered anticipatory, the prior art reference must be 

enabling and describe the applicant’s claimed invention sufficiently to have placed it in possession 

of a person of ordinary skill in the field of the invention.46 But, the degree of enabling detail 

contained in the reference does not have to exceed that contained in the patent at issue.47 

Further, the disclosure in the prior art reference does not have to be express, but may 

anticipate by inherency where the inherency would be appreciated by one of ordinary skill in the art.48 

To be inherent, the feature must necessarily be present in the prior art.49 Inherency may not be 

established by probabilities or possibilities. The mere fact that a certain thing may result from a given 

42 35 U.S.C. fj 102(b). 

43 35 U.S.C. fj 102(e). 

44 Texas Instruments, Inc. v. US. Int ’I Trade Comm ’n, 988 F.2d 1 165,1177 (Fed. Cir. 1993) 

45 Advanced Display Sys., Inc. v. Kent State Univ., 212 F.3d 1272, 1282 (Fed. Cir. 2000), 

46 Hellfx Ltd. v. Blok-Lok, Ltd., 208 F.3d 1339, 1346 (Fed. Cir. 2000) (“HeliJix”); In re 

47 Paulsen, 30 F.3d at 1481 n.9. 

48 Glaxo Inc. v. Novopharm Ltd., 52 F.3d 1043,1047 (Fed. Cir.), cert. denied, 516 U.S. 988 

49 See Finnigan Corp. v. US. Int ’I Trade Comm ’n, 180 F.3d 1354,1365-66 (Fed. Cir. 1999) 

(“Texas Instruments I.’). 

cert. denied, 532 U.S. 904 (2001) (“Advanced Display Systems”). 

Paulsen, 30 F.3d 1475, 1478 (Fed. Cir. 1994) (“Paulsen”). 

(1 995) (“Glaxo”). 

(“Finnigan”). 

14 
set of circumstances is not sufficient. If, however, the disclosure is sufficient to show that the natural 

result flowing from the operation as taught would result in the performance of the questioned 

function, it seems to be well settled that the disclosure should be regarded as sufficient. This modest 

flexibility in the rule that “anticipation” requires that every element of the claims appear in a single 

reference accommodates situations where the common knowledge of technologists is not recorded 

in the reference; that is, where technological facts are known to those in the field of the invention, 

albeit not known to 

2. Obviousness, 35 U.S.C. § 103 (a) 

Under 35 U.S.C. tj 103(a), a patent is valid unless “the differences between the subject matter 

sought to be patented and the prior art are such that the subject matter as a whole would have been 

obvious at the time the invention was made to a person having ordinary skill in the art to which said 

subject matter pertain^."^' The ultimate question of obviousness is a question of law, but “it is well 

understood that there are factual issues underlying the ultimate obviousness decision.”52 

Once claims have been properly construed, “[tlhe second step in an obviousness inquiry is to 

determine whether the claimed invention would have been obvious as a legal matter, based on 

underlying factual inquiries including : (1) the scope and content of the prior art, (2) the level of 

ordinary skill in the art, (3) the differences between the claimed invention and the prior art ; and (4) 

secondary considerations of non-obviousness” (also known as “objective e~idence”).~~ Although the 

50 See Cont’l Can Co. v. Monsanto Co., 948 F.2d 1264, 1268-69 (Fed. Cir. 1991) 

51 35 U.S.C. tj 103(a). 

52 Richardson-Vicks Inc., 122 F.3d at 1479; Wang Lab., Inc. v. Toshiba Corp., 993 F.2d 858, 

53 Smiths Indus. Med. Sys., Inc. v. Vital Signs, Inc., 183 F.3d 1347, 1354 (Fed. Cir. 1999) 

(continued ...) 

(“Continental Can ”); Finnigan, 180 F.2d at 1365. 

863 (Fed. Cir. 1993) (“ Wang Laboratories”). 

15 
Federal Circuit case law also required that, in order to prove obviousness, the patent challenger must 

demonstrate, by clear and convincing evidence, that there is a “teaching, suggestion, or motivation 

to combine, the Supreme Court has rejected this “rigid approach” employed by the Federal Circuit 

in KSR Int ’1 Co. v. Telejlex Inc. :54 

When a work is available in one field of endeavor, design incentives and other market 

forces can prompt variations of it, either in the same field or a different one. If a 

person of ordinary skill can implement a predictable variation, 0 103 likely bars its 

patentability. For the same reason, if a technique has been used to improve one device, 

and a person of ordinary skill in the art would recognize that it would improve similar 

devices in the same way, using the technique is obvious unless its actual application 

is beyond his or her skill. Sakraidaand Anderson’s-Black Rock are illustrative-a court 

must ask whether the improvement is more than the predictable use of prior art 

elements according to their established function. 

Following these principles may be more difficult in other cases than it is here 

because the claimed subject matter may involve more than the simple substitution of 

one known element for another or the mere application of a known technique to a 

piece of prior art ready for the improvement. Often, it will be necessary for a court to 

look to interrelated teachings of multiple patents; the effects of demands known to the 

design community or present in the marketplace; and the background knowledge 

possessed by a person having ordinary skill in the art, all in order to determine 

whether there was an apparent reason to combine the known elements in the fashion 

claimed by the patent at issue. To facilitate review, this analysis should be made 

explicitly. See In re Kahn, 441 F.3d 977, 988 (CA Fed. 2006) (“[Rlejections on 

obviousness grounds cannot be sustained by mere conclusory statements; instead, 

there must be some articulated reasoning with some rational underpinning to support 

the legal conclusions of obviousness”). As our precedents make clear, however, the 

analysis need not seek out precise teachings directed to the specific subject matter of 

the challenged claim, for a court can take account of the inferences and creative steps 

that a person of ordinary skill in the art would employ. 

The obviousness analysis cannot be confined by a formalistic conception of the words 

teaching, suggestion, and motivation, or by overemphasis on the importance of 

published articles and the explicit content of issued patents. The diversity of inventive 

53(. ..continued) 

( “Smiths Industries”), citing Graham v. John Deere Co., 383 U.S. 1, 17 (1 966) (“Graham”). 

54 KSR Int’l Co. v. Telefex Inc., 500 U.S. - (2007), 127 S.Ct. 1727, 1739 (“KSR”). 

16 
pursuits and of modern technology counsels against limiting the analysis in this way. 

In many fields it may be that there is little discussion of obvious techniques or 

combinations, and it often may be the case that market demand, rather than scientific 

literature, will drive design trends. Granting patent protection to an advance that 

would occur in the ordinary course without real innovation retards progress and may, 

in the case of patents combining previously known elements, deprive prior inventions 

of their value or utility.55 

“Secondary considerations,” also referred to as “objective evidence of non-obviousness,” such 

as “commercial success, long felt but unsolved needs, failure of others, etc.” may be used to 

understand the origin of the subject matter at issue, and may be relevant as indicia of obviousness or 

non-obvio~sness.~~ Secondary considerations may also include copying by others, prior art teaching 

away, and professional acclaim.57 

Evidence of “objective indicia of non-obviousness,” also known as “secondary 

considerations,” must be considered in evaluating the obviousness of a claimed invention, but the 

existence of such evidence does not control the obviousness determination. A court must consider 

all of the evidence under the Graham factors before reaching a decision on ~bviousness.~~ In order 

to accord objective evidence substantial weight, its proponent must establish a nexus between the 

evidence and the merits of the claimed invention, and aprima facie case is generally made out “when 

the patentee shows both that there is commercial success, and that the thing (product or method) that 

55 KSR, 500 U.S. at -; 127 S.Ct. at 1740-41. 

56 Graham, 383 U.S. at 17-18. 

57 See Perkin-Elmer Corp. v. Computervision Corp., 732 F.2d 888, 894 (Fed. Cir. 1984) 

(“Perkin-Elmer”), cert. denied, 469 U.S. 857 (1984); Avia Group Int’l, Inc. v. L.A. Gear California, 

853 F.2d 1557, 1564 (Fed. Cir. 1988) (“Avia”) (copying by others); In re Hedges, 783 F.2d 1038, 

1041 (Fed. Cir. 1986) (“Hedges”) (prior art teaching away; invention contrary to accepted wisdom); 

Kloster Speedsteel AB v. Crucible Inc., 793 F.2d 1565 (Fed. ir. 1986) (“Kloster”), cert. denied, 479 

U.S. 1034 (1987) (wide acceptance and recognition of the invention). 

58 Richardson-Vicks Inc., 122 F.3d at 1483-84. 

17 
is commercially successful is the invention disclosed and claimed in the patent.”59 Once the patentee 

has made aprima facie case of nexus, the burden shifts to the challenger to show that the commercial 

success was caused by “extraneous factors other than the patented invention, such as advertising, 

superior workmanship, etc.”60 

3. Written DescriptiodEnablement, 35 U.S.C. Q 112,y 1 

Section 112,l 1 of Title 35 requires that the specification describe the manner and process 

of making and using the invention “in such full, clear, concise, and exact terms as to enable any 

person skilled in the art to which it pertains, or with which it is most nearly connected, to make and 

use the same.” 

The issue of whether a disclosure is enabling is a matter of law.61 “To be enabling, the 

specification of a patent must teach those skilled in the art how to make and use the full scope of the 

claimed invention without ‘undue experimentation.”’6z “Patent protection is granted in return for an 

enabling disclosure of an invention, not for vague, intimations of general ideas that may or may not 

be workable.”63 Although a specification need not disclose minor details that are well known in the 

art, “[ilt is the specification, not the knowledge of one skilled in the art, that must supply the novel 

aspects of an invention in order to constitute adequate enablement,” and in so doing the specification 

59 In re GPAC Inc., 57 F.3d 1573,1580 (Fed. Cir. 1995) (“GPAC”); Demaco Corp. v. F. Von 

LangsdorffLicensingLtd., 851 F.2d 1387,1392 (Fed. Cir. 1988), cert. denied, 488 U.S. 956 (1988) 

(“Demaco”); Certain Crystalline Cefadroxil Monohydrate, Inv. No. 337-TA-293, Commission 

Opinion (March 15, 1990),15 U.S.P.Q.2d 1263, 1270 (“Certain Crystalline”). 

Id. at 1393. 

61 Applied Materials, Inc. v. Advanced Semiconductor Materials America, Inc., 98 F.3d 

Genentech, Inc. v. Novo Nordisk, A/S, 108 F.3d 1361,1365 (Fed. Cir. 1997) (“Genentech”). 

1563, 1575 (Fed. Cir. 1996) (“Applied Materials”). 

63 Id. at 1366. 
cannot merely provide “only a starting point, a direction for further research.”@ On the other hand, 

“[ilt is not fatal if some experimentation is needed, for the patent document is not intended to be a 

production spe~ification.”~~ “Undue experimentation” is “a matter of degree” and “not merely 

quantitative, since a considerable amount of experimentation is permissible, if it is merely routine, 

or if the specification in question provides a reasonable amount of guidance with respect to the 

direction in which the experimentation should proceed ....”66 

It is well-settled that in order to be enabling under Section 112, “the patent must contain a 

description sufficient to enable one skilled in the art to make and use the full scope of the claimed 

in~ention.”~~ Section 1 12 requires that the scope of the claims must bear a reasonable correlation to 

the scope of enablement provided by the specification to such persons.68 

4. Best Mode, 35 U.S.C. 0 112,y 1 

Section 112,v 1 of Title 35 of the United States Code sets out the best mode requirement, 

stating in relevant part that “[tlhe specification shall contain . . . and shall set forth the best mode 

contemplated by the inventor of carrying out the in~ention.”~~ TheCourt of Appeals for the Federal 

Circuit has held that “[tlhe purpose of the best mode requirement is to ensure that the public, in 

exchange for the rights given the inventor under the patent laws, obtains from the inventor a full 

64 Id. 

65 Northern Telecom, Inc. v. Datapoint Corp. , 908 F.2d 93 1,941 (Fed. Cir. 1990) (“Northern 

Telecom”). 

66 PPG Industries, Inc. v. Guardian Industries Corp., 75 F.3d 1558, 1564 (Fed. Cir. 1996) 

(L‘PPG Industries”). 

67 Unitedstates v. Teletronics, Inc., 857 F.2d 778,785 (Fed. Cir. 1988) (“Teletronics”); see 

also Amgen, Inc. v. Chugai Pharmaceutical Co., Ltd., 927 F.2d 1200, 1213 (Fed. Cir. 1991) 

(“Chugai”) (inventor’s disclosure must be “sufficient to enable on skilled in the art to carry out the 

invention commensurate with the scope of his claims”). 

Application of Fischer, 427 F.2d 833,839 (C.C.P.A. 1970) (“Fischer”). 

69 35 U.S.C. 9 112 ‘1T 1. 

19 
disclosure of the preferred embodiment of the in~ention.”~’ The determination of whether the best 

mode requirement is satisfied is a question of fact, which must be proven by clear and convincing 

evidence.71 

In determining compliance with the best mode requirement, two inquires are undertaken. The 

first inquiry is whether, at the time of filing the patent application, the inventor considered aparticular 

mode of practicing the invention superior to all other modes.72 This first inquiry is subjective and 

focuses on the inventor’s state of mind at the time the patent application was filed. The second 

inquiry is whether the inventor’s disclosure is adequate to enable one of ordinary skill in the art to 

practice the best mode of the invention. This second inquiry is objective and depends on the scope 

of the claimed invention and the level of skill in the relevant art. 

The “contours of the best mode requirement are defined by the scope of the “claimed 

invention” and thus, the first task in any best mode analysis is to define the invention.73 “The 

definition of the invention, like the interpretation of the patent claims, is a legal exercise, wherein the 

ordinary principles of claim construction apply.”74 Once the invention is defined, the best mode 

inquiry moves to determining whether a best mode of carrying out that invention was held by the 

70 Dana Corp. v. IPC Ltd. Partnership, 860 F.2d 41 5,4 18 (Fed. Cir. 1988), cert. denied, 490 

U.S. 1067 (1989) (“Dana Corp.”). 

71 Transco Products Inc. v. Performance Contracting, Inc., 38 F.3d 55 1,559-60 (Fed. Cir. 

1994) (“Transco”). 

72 See LiquidDynamics Corp. v. Vaughan Co., Inc., 449 F.3d 1209, 1223 (Fed.Cir. 2006); 

see also Spectra-Physics, Inc. v. Coherent, Inc., 827 F.2d 1524, 1535 (Fed. Cir. 1987) (The 

specificity of disclosure necessary to’meet the best mode requirement is determined “by the 

knowledge of facts within the possession of the inventor at the time of filing of the application.”) 

(“Spectra-Physics”). 

73 Northern Telecom Ltd. v. Samsung Electronics Co., Ltd., 215 F.3d 1281, 1286-87 (Fed. 

Cir. 2000). 

74 Id. 

20 
inventor. If so, that best mode must be disclosed. In Pfizer, Inc. v. Teva Pharmaceuticals USA, Inc., 

518 F.3d 1353 (Fed. Cir. 2008), the Federal Circuit summarized its best mode jurisprudence as 

follows: 

We held that the best mode requirement does demand disclosure of an inventor’s 

preferred embodiment of the claimed invention. However, it is not limited to that. 

We have recognized that best mode requires inventors to disclose aspects of making 

or using the claimed invention [when] the undisclosed matter materially affects the 

properties of the claimed in~ention.~~ 

B. Inequitable Conduct 

A patent is unenforceable on grounds of “inequitable conduct” if the patentee withheld 

material information from the PTO with intent to mislead or deceive the PTO into allowing the 

claims.76 Both materiality and intent must be proven by clear and convincing evidence.77 When 

inequitable conduct occurs in relation to one or more claims of a patent, the entire patent is 

unenforceable. 78 

According to the rules of the PTO, the duty to disclose information “exists with respect to 

each pending claim until the claim is canceled or withdrawn from consideration, or the application 

becomes abandoned. Information material to the patentability of a claim that is canceled or withdrawn 

from consideration need not be submitted if the information is not material to the patentability of any 

claim remaining under consideration in the application. There is no duty to submit information which 

75 Pfizer, 5 18 F.3d at 1364 (internal quotations and citations omitted). 

76 LaBounty MJ., Inc. v. US. Int’l Trade Comm‘n, 958 F.2d 1066, 1070-1074 (Fed. Cir. 

1992) (“LaBounty”). 

77 Id.; Kingsdown Med. Consultants, Ltd. v. Hollister, Inc., 863 F.2d 867, 872 (Fed. Cir. 

1988), cert. denied, 490 U.S. 1067 (1 989) (“Kingsdown”); Certain Salinomycin Biomass and 

Preparations Containing Same, Inv. No. 337-TA-370, Unreviewed Initial Determination at 76,1995 

WL 1049822 (U.S.I.T.C. November 6,1999, afdsub nom. Kaken Pharmaceutical Co., Ltd. v. US. 

Int’l Trade Comm’n, 11 1 F.3d 143 (Fed. Cir. 1997) (Table) (nonprecedential) (“Salinomycin”). 

78 Kingsdown, 863 F.2d at 874. 

21 
is not material to the patentability of any existing claim.”79 

Generally, when withheld information is highly material, a lower showing of deceptive intent 

will be sufficient to establish inequitable conduct.go Moreover, “[dlirect proof of wrongful intent is 

rarely available but may be inferred from clear and convincing evidence of the surrounding 

circum~tances.”~~ Theconduct at issue must be viewed in light of all the evidence, including evidence 

of good faith.82 

“Information is material where there is a substantial likelihood that a reasonable examiner 

would consider it important in deciding whether to allow the application to issue as a patent.”83 A 

patent applicant, however, has no obligation to disclose areference that is cumulative or less pertinent 

than those already before the examiner.84 Under the rules of the PTO, information is material when 

it is not cumulative to information of record and it either (i) “establishes, by itself or in combination 

with other information, a prima facie case of unpatentability of a claim”; or (ii) “it refutes, or is 

inconsistent with, a position the applicant takes” in either opposing the PTO’s argument of 

unpatentability or asserting the applicant’s own argument of ~atentability.~~ Close cases, however, 

“should be resolved by disclosure, not unilaterally by applicant.”86 

79 37 C.F.R. 0 1.56(a). 

American Hoist & Derrick Co. v. Sowa & Sons, Inc., 725 F.2d 1350,1363 (Fed. Cir.), cert. 

denied, 469 U.S. 821 (1984) (“American Hoist”). 

” LaBounty, 958 F.2d at 1076; Salinomycin, ID at 77. ’* Kingsdown, 863 F.2d at 876; Salinomycin, ID at 77. 

83 LaBounty, 958 F.2d at 1074; Salinomycin, ID at 77. 

84 Halliburton Co. v. Schlumberger Tech. Corp., 925 F.2d 1435, 1439-40 (Fed. Cir. 1991) 

85 37 C.F.R. § 1.56(b). 

86 Abbott Laboratories v. TorPharm, Inc., 300 F.3d 1367, 1379 (Fed. Cir. 2002) 

(“Halliburton”) . 

(“TorPharm”) quoting LaBounty, 958 F.2d at 1076. 

22 
C. Unclean Hands 

The unclean hands doctrine provides that a court’s equitable power “can never be exerted on 

behalf of one who has acted fraudulently, or who by deceit or any unfair means has gained an 

advantage.”87 Courts will only apply-the doctrine when it has been shown that the inequitable conduct 

bears “an immediate and necessary relation to the equity” that the patent holder seeks in litigation.88 

Unclean hands must be proven by clear and convincing evidence.89 

IV. The ‘160 Patent 

A. Claim Construction 

1. Asserted Claims 

Claim 15 is the only asserted claim of the ‘ 160 patent. Claim 15 of the ‘ 160 patent depends 

from independent claim 3. Claim 15 reads as follows: 

1 5. A method of producing L-lysine, comprising: 

cultivating the bacterium of claim 3 in a suitable culture medium, 

producing and accumulating L-lysine in the culture thereof, and 

collecting L-lysine from the culture.90 

Independent claim 3 reads as follows: 

3. A bacterium belonging the genus Escherichia which is transformed with a 

DNA coding for a dihydrodipicolinate synthase originating from a bacterium 

belonging to the genus Escherichia and having mutation to desensitize feedback 

87 Keystone Driller Co. v. General Excavator Co., 290 US. 240,245 (1 933). 

88 Certain Home Vacuum Packaging Products, 337-TA-496,2004 WL 1082507, Notice at 

88-89 (March 2004); see also Precision Instrument Mfg., Co. v. Automotive Maint. Mach. Co., 324 

U.S. 806,815 (1945). 

89 In re Omeprazole Patent Litigation, 483 F.3d 1364,1374 (Fed. Cir. 2007) (“Andrx bears 

the burden of proving by clear and convincing evidence that Astra acted with unclean hands.”). 

Notably, GBT incorrectly asserts in its post-hearing brief that the standard is preponderance of the 

evidence. See RIB at 69. 

90 JX-1 at 68:l-5. 

23 
inhibition by L-lysine, wherein the mutation is selected from the group consisting of 

(a) a mutation to replace the alanine residue at the 81st position as 

counted from the N-terminal in the amino acid sequence of the 

dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue, 

(b) a mutation to replace the histidine residue at the 1 18th position as 

counted from the N-terminal in the amino acid sequence of the 

dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue, and 

(c) a mutation to replace the alanine residue at the 81st position as 

counted from the N-terminal in the amino acid sequence of the 

dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue and replace the histidine residue at the 1 18th position as 

counted from the N-terminal in the amino acid sequence of the 

dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue, 

(d) a mutation to replace the alanine residue corresponding to the 8 1 st 

position as counted from the N-terminal in the amino acid sequence of 

the dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue, 

(e) a mutation to replace the histidine residue corresponding to the 

11 8th position as counted from the N-terminal in the amino acid 

sequence of the dihydrodipicolinate synthase of SEQ ID NO: 4 with 

another amino acid residue, and 

(f) a mutation to replace the alanine residue corresponding to the 8 1 st 

position as counted from the N-terminal in the amino acid sequence of 

the dihydrodipicolinate synthase of SEQ ID NO: 4 with another amino 

acid residue and replace the histidine residue corresponding to the 

118th position as counted from the N-terminal in the amino acid 

sequence of the dihydrodipicolinate synthase of SEQ ID NO: 4 with 

another amino acid re~idue.~' 

91 JX-1 at 61:43-62:18. 

24 
2. Disputed Claim Limitations 

There are no disputed claim limitationsper se. However, GBT and the Staff argue that the 

‘ 160 patent at issue is invalid for failing to satis@ the best mode requirement of 35 U.S.C. 5 1 12. As 

previously stated, the contours of the best mode analysis are defined by the scope of the claimed 

invention, which in turn is determined by applying the ordinary principles of claim construction. 

Thus, in this regard, the parties do dispute how the scope of the claimed invention is construed. 

However, this dispute is more appropriately resolved, infra, when analyzing GBT and the Staffs best 

mode argument.92 

B. Infringement 

Ajinomoto and GBT stipulate that GBT’s manufacture of L-lysine feed products using the Old 

Escherichia bacterium strain deposited with the ATCC under Accession #SD-5590 infringes claim 

15 of the ‘ 160 patent.93 Ajinomoto and GBT also stipulate that GBT’s manufacture of L-lysine 

products using the Corynebacterium strain deposited with the ATCC under Accession #SD-5620 does 

not infringe Claim 15 of the ‘ 160 patent.94 Additionally, Ajinomoto and GBT stipulate that GBT’s 

manufacture of L-lysine products using the New Escherichia bacterium strain deposited with the 

ATCC under Accession #SD-57 17 does not infringe Claim 15 of the ‘ 160 patent.95 Based on the 

stipulation, the undersigned finds that: (1) GBT’s manufacture of L-lysine feed products using the 

Old Escherichia bacterium strain deposited with the ATCC under Accession #SD-5590 infringes 

92 Ajinomoto and GBT accuse each other of impermissibly trying to read into claim 15 of 

the ‘160 patent a large scale production limitation. However, both parties admit that no such 

limitation exists. Thus, there does not appear to be a dispute on this point. See CIB at 14-16; RIB 

at 11. 

93 JX- 190C at 7 9. 

94 Id. at711. 

95 Id. at 7 12. 

25 
claim 15 of the ' 160 patent; (2) GBT's manufacture of L-lysine products using the Corynebacterium 

strain deposited with the ATCC under Accession #SD-5620 does not infringe Claim 15 of the ' 160 

patent; and (3) GBT's manufacture of L-lysine products using the New Escherichia bacterium strain 

deposited with the ATCC under Accession #SD-5717 does not infringe Claim 15 of the ' 160 patent. 

C. 

Ajinomoto and GBT stipulate that Heartland uses the method of Claim 15 of the ' 160 patent 

to make L-lysine products.96 Based on the stipulation, the undersigned finds that Ajinomoto practices 

claim 15 of the ' 160 patent. Accordingly, the undersigned finds that Ajinomoto satisfies the technical 

prong of the domestic industry requirement of Section 337 with regard to the asserted '160 patent. 

Domestic Industry - Technical Prong 

D. Validity 

1. Ordinary Skill in the Art 

Ajinomoto asserts that one of ordinary skill in the art as of the time of the invention would 

have an advanced degree in chemical or agricultural engineering or microbiology with specialization 

in metabolic engineering, or a related field, or at least several years of concentrated study or work in 

the field of bacteriology and strain development in connection with fermentationtechnique^.^^ GBT 

asserts that one of ordinary skill in the art is a person with at least a master's level degree in some 

kind of biological science, probably focused around molecular biology, genetics, microbiology and 

has practical experience, that is, hands-on experience in a research lab that was performing 

recombinant DNA work.98 GBT also asserts that individuals trained to the Bachelor's level could also 

be skilled in the art, but only after on-the-job training under the direct supervision of a Ph.D.-level 

96 Id. at 7 5. 

97 CX-231C (Liao WS) at 7 50. 

98 RX-89C (Webb WS) at f 292. 

26 
scientist.99 Staff asserts that one of ordinary skill in the art is a person with an advanced degree in 

Biology, Biochemistry, Genetics, Genomics, Microbiology, Molecular Biology, Agricultural 

Engineering, Metabolic Engineering with 3-5 years of experience in a laboratory specializing in 

genetic engineering. The Staff also asserts that individuals trained to the Bachelor's level could also 

be skilled in the art, but only after on-the-job training under the direct supervision of a Ph.D.-level 

scientist."' The undersigned agrees with the Staff that a person of ordinary skill in the art to which 

the '160 patent pertains would have an advanced degree in Biology, Biochemistry, Genetics, 

Genomics, Microbiology, Molecular Biology, Agricultural Engineering, Metabolic Engineering with 

3-5 years of experience in a laboratory specializing in genetic engineering. The undersigned also 

agrees with the Staff that persons with a Bachelor's degree could also be skilled in the art, but only 

after on-the-job training under the direct supervision of a Ph.D.-level scientist. 

2. Best Mode 

The first task in the best mode analysis is to define the invention claimed in the ' 160 patent. 

Ajinomoto argues that the inventors of the ' 160 patent fully disclosed the invention and the best mode 

of carrying it out by disclosing the best mode of making the specific mutations to the dapA gene to 

encode a DDPS enzyme desensitized to feedback inhibition by lysine."' Ajinomoto argues that where 

the claims contain limitations that do not distinguish the claimed invention from the prior art, those 

limitations are irrelevant to the best mode analysis.''* Thus, while Ajinomoto acknowledges that 

independent claim 3, on which asserted claim 15 depends, refers to a "bacterium," Ajinomoto argues 

99 RX-88C (Somerville WS) at 7 3 1. 

loo SFF 317 (citing Somerville, Tr. at 884-86; RX-88C (Somerville WS) at 7 31; CX-231 

(Liao WS) at 7 50). 

lo' CIB at 9. 

lo* Id. 

27 
that because the claim limitation of a “bacterium” does not distinguish the invention of the ‘160 

patent from the prior art, the best mode analysis should focus on the novel elements of the claims, viz. 

the specific genetic modifications to the dapA gene.’03 Specifically, Ajinomoto argues that “it is 

irrelevant that the claims-at-issue are directed to a method of producing lysine, because the ‘best 

mode’ analysis focuses only on the novel mutation^."'^^ According to Ajinomoto, the inventors did 

not claim a novel bacterium. Instead, it is asserted that the inventors claimed any bacterium of the 

genus Escherichia that contains the specific mutations to the dapA gene. In support of its argument, 

Ajinomoto relies on several cases: Christianson v. Colt Indus. Operating Corp., 822 F.2d 1544 (Fed. 

Cir. 1987) (“Christianson”); Monon Corp. v. Stoughton Trailers, Inc., 1999 WL 335 10001 (N.D. Ill., 

Sept. 27, 1999) ((‘Monon’’); and Spalding & EvenjZo Cos. v. Acushnet Co., 718 F.Supp. 1023 (D. 

Mass. 1989)(“Spalding”). Ajinomoto asserts that in each of these cases, the court performed the best 

mode analysis on the part of the claimed invention that defined its novelty and asked whether the 

inventors disclosed the best mode as to that part.lo5 Ajinomoto argues that the same analysis should 

be applied in this investigation in finding that the scope of the best mode inquiry is only the novel 

gene mutations claimed in the ‘ 160 patent.lo6 

GBT argues that the claims of the ‘160 patent are drawn to lysine production using a 

micro~rganism.’~~ Specifically, GBT argues that claim 3, on which asserted claim 15 depends, 

explicitly recites the limitation “bacterium belonging to the genus Escherichia.”108 According to 

lo3 Id. at 10. 

lo4 Id. at 17. 

lo5 CIB at 14. 

lo6 Id. 

IO7 RIB at 12. 

IO8 Id. 

28 
GBT, the "bacterium" is the host. GBT argues that Ajinomoto's proposed construction ofthe claimed 

invention as being limited to the dapA gene should be rejected because it reads limitations out of the 

~lairns.''~ 

The Staff argues that the scope of the claimed invention of the ,160 patent includes the 

bacterium (i. e., host), the specific mutation, the medium and whatever else is required to produce 

Lysine using a fermentation process and collecting it after it has been produced."' Specifically, the 

Staff argues that claim 3, on which asserted claim 15 depends, expressly requires a Escherichia 

bacteria having the following mutation(s): a replacement of the alanine residue that is normally the 

8 1 st amino acid within the wild-type amino acid sequence of SEQ ID NO: 4; and/or replacement of 

the histidine residue that is normally the 1 18th amino acid within the wild-type amino acid sequence 

of SEQ ID NO: 4."' According to the Staff, the claimed mutation(s) are to the dapA gene, which 

regulates production of DDPS.'12 The Staff argues that asserted claim 15 expressly encompasses 

production of lysine produced by E. coli bacteria having the above described mutation(s) in a liquid 

fermentation medium.113 

Id. 

'lo SIB at 18. 

SIB at 17. 

'I2 Id. 

'I3 Id. Both GBT and the Staff assert that Ajinomoto failed to include in its pre-hearing brief 

its argument that only the novel elements of a claim are subject to the best mode requirement and 

thus, GBT and the Staff argue that pursuant to Ground Rule 8.2, Ajinomoto has waived any such 

argument. See RRB at 2-3; SRB at 2 n.3. Ajinomoto asserts consistently in its pre-hearing brief that 

the claimed invention is limited to the mutation to the dapA gene and does not include the host 

bacterium. See CPHB at 20-22. The undersigned finds Ajinomoto's argument in its post-hearing 

brief that only the novel elements of a claim are subject to the best mode requirement and thus the 

bacterium in claim 15 of the ' 160 patent should not fall within the contours of the best mode analysis 

sufficiently implicated by Ajinomoto's assertion in its pre-hearing brief that the claimed invention 

is limited to the mutation to avoid running afoul of Ground Rule 8.2. Accordingly, the undersigned 

(continued ...) 

29 
“The definition of the invention, like the interpretation of the patent claims, is a legal exercise, 

wherein the ordinary principles of claim construction apply.”114 Looking first to the claims of the 

‘160 patent, the undersigned finds that the preamble language of asserted claim 15 clearly and 

unambiguously sets forth the utility of the claimed invention, namely “producing L-ly~ine.””~ As set 

forth in claim 15, the production of L-lysine includes at least the following three steps: (1) cultivating 

the bacterium of claim 3 in a suitable culture medium (ie., A bacterium belonging to the genus 

Escherichia having a mutation to the dapA gene to desensitize feedback inhibition by L-lysine.); (2) 

producing and accumulating L-lysine in the culture thereof; and (3) collecting L-lysine from the 

culture.Il6 Thus, according to the plain language of claim 15, the claimed invention includes the 

overall production of L-lysine, as well as, the cultivation of an Escherichia bacterium with the specific 

mutation to the dapA gene, and the accumulation and collection of the L-lysine. 

Having examined the claims, the specification is consulted. The specification confirms that 

the invention of the ‘ 160 patent is not simply directed to the mutation to the dapA gene, but to a 

bacterium belonging to the genus Escherchia having the mutation to the dapA gene and an improved 

method for producing L-lysine using said bacterium. For example, the specification states that “[tlhe 

present invention has been made taking the aforementioned viewpoints into consideration, an object 

of which is to obtain DDPS and AKIII originating from bacteria belonging to the genus Escherichia 

’ 13(.. .continued) 

finds Ajinomoto’s argument was not waived. 

‘I4 Northern Telecom, 215 F.3d at 1286-87; see also Engel Indus., Inc. v. Locvormer Co., 

946 F.2d 1528, 1531 (Fed. Cir. 1991)c‘The best mode inquiry is directed to what the applicant 

regards as the invention, which in turn is measured by the claims.”). 

‘I5 See Northern Telecom, 2 15 F.3d at 1287 n. 1 (“Preamble language in a claim may provide 

an indication of how the inventor intended to ‘carry out’ his invention.”). 

‘I6 See JX-1 at 61:43-62:37,68:1-5. 

30 
with sufficiently desensitized feedback inhibition by L-lysine, and provide a method of producing Llysine by fermentation which is more improved than those in the prior art.”117 The Federal Circuit 

has recognized that the use of the phrase “present invention” puts the public on notice as to the scope 

of the invention as a whole.”8 

Thus, based on the plain language of the claims, as supported by the specification, the 

undersigned finds the claimed invention of claim 15 of the ‘160 patent to encompass the overall 

production of L-lysine, including the cultivation of an Escherichia bacterium with the specific 

mutation(s) to the dapA gene, and the accumulation and collection of the L-lysine. 

Ajinomoto does not dispute that claim 15 of the ‘160 patent expressly encompasses 

production of lysine from a bacteria of the genus Escherichia having the specific mutations to the 

dapA gene in a liquid fermentation medium.”’ Instead, Ajinomoto argues that only the novel aspects 

of a claimed invention, which in this instance Ajinomoto asserts is the mutation to the dapA gene, 

are subject to the best mode requirement of section 112. Ajinomoto finds support for its argument 

in the following cases: (1) Christianson; (2) Monon; and (3) Spalding. 

‘I7 See JX-1 at 2:56-62; see also id. at 1: 1-2 (“METHOD OF PRODUCING L-LYSINE BY 

FERMENTATION”), 3:36-50 (“The present invention further lies in a bacterium belonging to the 

genus Escherichia . . .”), 4:66-5:4 (“The present invention further provides a method of producing 

L-lysine comprising the steps of cultivating any of the bacterium belonging to the genus Escherichia 

described above in an appropriate medium, producing and accumulating L-lysine in a culture thereof, 

and collecting L-lysine from the culture.”). 

‘I8 See, e.g., Honeywell Int ’I Inc. v. ITT Indus., Inc., 452 F.3d 13 12, 13 18 (Fed. Cir. 2006); 

Alloc, Inc. v. US. Int‘I Trade Comm’n, 342 F.3d 1361, 1378 (Fed. Cir. 2003). 

See SFF81 (no dispute); SFF84 (no dispute); CFF4.14 (“Thus, the invention claimed by 

Claim 15 of the ‘ 160 Patent is the culture, production and collection of lysine from an Escherichia 

organism having one or both of two specific mutations of the dapA gene that reduce or eliminate 

feedback inhibition of the DPPS enzyme.”); CFF5.3 (“Claim 3 describes the bacterium with 

reference to two specific mutations that alter the amino acid sequence in an enzyme (DDPS) encoded 

by the dapA gene.”); see also CIB at 12 (“[Tlhey claimed a bacterium. . . that contains the specific 

mutation to the dapA gene.”). 

31 
As discussed in more detail below, the undersigned does not find that either Christianson or 

Monon supports Ajinomoto’s argument. While Spalding on the other hand “arguably” does support 

Ajinomoto’s position, the undersigned finds the reasoning of the district court in Spalding to be 

contrary to the best mode jurisprudence of the U.S. Court of Appeals for the Federal Circuit and 

consequently finds the case unpersuasive. The fact is, the undersigned has been unable to locate any 

Federal Circuit case where the Court ignored an express claim limitation in determining whether the 

best mode requirement was satisfied. 

Christianson involved patents directed to various parts of a rifle. Christianson argued that 

Colt violated the best mode requirement of section 1 12 by failing to disclose the dimensions and 

tolerances necessary to mass produce an M-16 rifle. The district court agreed. The Federal Circuit 

reversed. In holding that Colt did not violate the best mode requirement, the Federal Circuit stated: 

In this case, interchangeability with M-16 parts appears nowhere as a limitation in any 

claim, and as Christianson concedes, the patents make no reference whatever to the 

M- 16 rifle. Thus the best mode for making and using and carrying out the claimed 

inventions does not entail or involve either the M- 16 rifle or interchangeability. The 

“best mode” for making and using the claimed parts relates to their use in a rifle, any 

rifle. There is nothing anywhere in the present record indicating that any of the 

patents fail to meet that requirement.I2O 

In contrast with Christianson, asserted claim 15 of the ‘ 160 patent expressly includes a bacterium 

with the specific mutation to the dapA gene. Thus, unlike the unclaimed M- 1 6 rifle in Christianson, 

the bacterium in claim 15 is expressly claimed and thus within the contours of the best mode analysis. 

Monon involved a patent which disclosed a design for the sidewalls that extend the length of 

an over-the-road trailer (a.k.a., “eighteen wheeler”).’*’ Claim 1 of the patent at issue in Monon states: 

120 Christianson, 822, F.2d at 1563 (emphasis in original). ’*’ Monon, 1999 WL at * 1 -*2. 

32 
A trailer body construction comprising . . . a plurality of similar, generally flat 

rectilinear side panels of lightweight metallic material . . . and a plurality of joining 

panels of second lightweight metallic material situated only on one surface of each 

sidewall for joining, and strengthening respective adjacent pairs of said side walls . . . and a plurality of fasteners for coupling said joining panels to respective adjacent 

pairs of said side panels to both join and strengthen said side 

Respondent Stroughton argued that Monon violated the best mode requirement by failing to disclose 

both its best known joining panel design (one that apparently was lighter in weight than the one 

disclosed in the patent) and its design for sealing the side ~ane1s.I~~ The district court disagreed. The 

district court found the elements Stroughton alleged violated the best mode requirement were not 

claimed in the patent at issue. Specifically, in finding that Monon did not violate the best mode 

requirement, the district court stated: 

The focus of the best mode requirement is on the claimed invention. Nowhere in the 

claims is it stated that the invention is to be leakage-proof, nor do the claims state that 

the invention has to be lightweight. As stated above, the claimed invention relates to 

a trailer that maintains desired structural sidewall strength with a minimized interior 

width.'24 

In contrast to the unclaimed elements in Monon, asserted claim 15 of the '160 patent expressly 

includes a bacterium with the specific mutation to the dapA gene. Because the bacterium is expressly 

claimed, it is within the contours of the best mode analysis. To hold otherwise would be to 

impermissibly read a limitation out of a claim. 

Spalding involves a patent with the following asserted claim: 

a golf ball comprising a core and a cover, wherein said cover comprises . . . from 

about 10 to about 90 percent of an ionic copolymer of an olefin having from 2 to 5 

carbon atoms and a zinc salt of an unsaturated monocarboxylic acid containing from 

'22 Id. at *18. 

123 Id. at *19. 

124 Id. (internal citation omitted). 

33 
3 to 8 carbon atoms.’25 

Respondent Acushnet argued that the patent was invalid for failing to comply with the best mode 

requirement by: (1) failing to set forth the core material which was used in the Spalding two-piece 

Top Flite ball upon which ball the cover material of blended ionic copolymers gave the greatest 

advantage; and (2) failing to disclose the processing conditions required to produce the best exemplar 

of Spalding’s two-piece golf In addressing Acushnet’s argument, the district court stated that 

“[tlhe invention is not the golf ball but ‘[a] golf ball comprising a core and a cover.”’ Although the 

district court correctly noted that the asserted claim included limitations directed to both a core and 

a cover, confusingly, the district court found that the claimed invention was only the golf ball cover. 

In so finding, the district court stated: 

The law requires that the inventor disclose the best mode for making the claimed part 

of the invention, not every other part of the product to which the claimed part is 

attached. The specification of the Molitor patent points out in 22 places that the cover 

is the invention, beginning with the title “Golf Ball Cover Composition Comprising 

A Mixture of Ionomer Resins.” Prior art claims read on golf balls and two piece golf 

balls. Nowhere in the claims of the Molitor patent is it stated that the Molitor 

invention purports to be a two-piece golf ball. 

Contrary to the district court’s statement, Federal Circuit best mode jurisprudence is quite clear that 

the scope of the best mode analysis is defined by the claimed invention, not the claimed part of the 

invention as stated by the district court. Moreover, while the district court stated that nowhere in the 

claims of the patent does it state that the invention purports to be a two-piece golf ball, the claim 

language is explicitly drawn to both a core and a cover. The Federal Circuit has stated that “[tlhe 

definition of the invention, like the interpretation of the patent claims, is a legal exercise, wherein the 

Spalding, 718 F.Supp at 1027 

126 Id. at 1048-49. 

34 
ordinary principles of claim construction apply.”127 Here the district court failed to apply the ordinary 

principles of claim construction by ignoring the express claim language directed to the core. 

Accordingly, the undersigned finds Spalding unpersuasive. 

Having defined the invention of claim 15 of the ‘ 160 patent, the undersigned turns to GBT’s 

specific arguments supporting its contention that there has been a violation of the best mode 

requirement with regard to claim 15 of the ‘ 160 patent. GBT makes two separate arguments: (1) that 

the Ajinomoto inventors failed to disclose their preferred host strain; and (2) that the disclosed best 

mode was fictitious.I2’ Each argument will be addressed in turn below. 

a. The Ajinomoto inventors failed to disclose their preferred host 

strain 

GBT and the Staff argue that in December 1993, the inventors believed that the EA-70 was 

the best host strain for practicing claim 15.’29 In support of their argument, GBT and the Staff 

primarily rely on contemporaneous statements made by the inventors in their lab notebooks and in 

various monthly reports and research report^.'^' GBT asserts that inventors’ testimony at the hearing 

repudiated much of their testimony given during their depositions earlier in the in~estigation.’~’ GBT 

argues that the inventors’ “new opinions” are less credible than the documentary record and 

deposition testimony and accordingly should be rejected.’32 While GBT and the Staff acknowledge 

that the documentary evidence does mention that the AE-70 strain had some flaws, GBT and the Staff 

argue that, notwithstanding its flaws, the documentary evidence repeatedly refers to AE-70 as the 

127 Northern Telecom, 215 F.3d at 1286-87. 

12’ RIB at 16, 28. 

130 RIB at 19-20; SIB at 27-33. 

131 RIB at 22. 

132 Id. 

RIB at 16; SIB at 27. 

35 
“best,” “highest,” and GBT also notes that at times, AE-70 was simply referred to as 

“the” or the “sole” lysine-producing strain.’34 Additionally, GBT and the Staff argue that in some of 

the documentary evidence, the inventors made explicit comparisons between AE-70 and other strains 

and stated that AE-70 was better.135 Further, GBT and the Staff note that even after the December 

1993 effective filing date of claim 15 of the ‘ 160 patent, Ajinomoto continued to work with the AE70 strain. 136 

Ajinomoto argues that when the Japanese application was filed on December 8, 1993, the 

inventors disclosed what they believed to be the best strains for showing that their invention worked, 

viz., the B-3996 and W3 1 lO(tyrA) strains.’37 With regard to AE-70, Ajinomoto argues that as of the 

December 8, 1993 filing date of the Japanese priority application, Dr. Kojima and his colleagues 

knew AE-70 was a flawed strain that was unsuitable for Ajinomoto purposes.’38 Ajinomoto asserts 

that AE-70 was [ 

Ajinomoto argues that GBT and the Staff 

“cherrypicks” Ajinomoto’s internal documents for statements in the English translations 

characterizing AE-70 as “best” in terms of its accumulation.140 Ajinomoto argues that GBT and the 

Staffs reliance on accumulation of lysine to argue that the inventors subjectively considered AE-70 

the “best” host strain is improper, because the inventors considered other metrics important in 

133 RIB at 17; SIB at 12-15. 

134 RIB at 17. 

135 RIB at 20-21; SIB at 32-33. 

136 RIB at 18; SIB at 30. 

137 CIBat21. 

138 Id. 

‘39 Id. 

140 Id. at 8,24. 

36 
choosing a host strain.I4’ Ajinomoto also argues that the disclosed strains better demonstrated the 

effect of the amplification of specific genes, which Dr. Kojima believed was the essence of the ‘ 160 

patent.I4* Additionally, Ajinomoto argues that the relative effect of the patented mutations was 

greater in the disclosed strains then in AE-70.143 Further, Ajinomoto notes that AE-70 was discarded 

a few months after the December 1993 filing.144 

As discussed in detail below, the undersigned finds that the documentary evidence of record 

shows clearly and convincingly that the inventors subjectively considered the AE-70 strain the best 

host strain for practicing claim 1 5 of the ‘ 160 patent as of the effective filing date of December 1993. 

While AE-70 was not perfect, the evidence shows that AE-70 still fared better in practically all 

respects to the other host strains that the Ajinomoto inventors were working with at the time. 

Moreover, the evidence shows that the inventors still believed AE-70 to be their best host strain, even 

in light of its flaws. Section 112 best mode requirement calls for disclosure of the inventors’ 

preferred embodiment. Here the evidence clearly shows that the inventors had a preference for AE-70 

above all others as of December 1993. 

The Ajinomoto Lysine Project began in 1990.145 The project team at the time of its inception 

included Dr. Konosuke Sano (“Sano”), Dr. Hiroyuki Kojima (“Kojima”), Ms. Kazue Kawamura 

(“Kawamura”), and Ms. Yuri Ogawa (“Oga~a”).’~~ During the course of the Lysine Project, other 

Ajinomoto researchers participated in the project, including Yoshimi Kikuchi, Tomoko Suzuki, 

141 

142 

143 

144 

145 

146 

Id. at 25-27. 

Id. at 22. 

Id. at 22-23. 

Id. at 21. 

RFF 1.134 (no dispute). 

SFF 112 (no dispute). 

37 
Kazuo Nakanishi, Junichiro Kojima (“J. Kojima”), and Yasushi Ni~himura.’~~ Sano and Kojima 

worked primarily on determining what genetic mutations would have to be made in order to optimize 

the E.coli bacteria for Lysine prod~ction.’~’ Ogawa and Kawamura were principally focused on 

developing culturing techniques and searching for host strains for the genetic modifications Sano and 

Kojima were hoping to discover.149 Kojima left the Lysine Project in March 1992 to work on another 

project and returned to the Lysine Project in April 1993.l5’ At the beginning of the project Sano was 

the Project Leader.”’ After returning to the Lysine Project in April 1993, Kojima became Project 

Leader. 152 

The researchers assigned to Ajinomoto’s Lysine Project created two different types of reports, 

a monthly report and a research report. Monthly reports included single page reports authored by each 

of the researcher^.'^^ Research reports were prepared only after milestones were reached.154 

As previously stated, the Lysine Project began in 1990. In the October 1990 monthly report, 

Kawamura reported that she had performed preliminary experimentation on the following strains to 

determine which strains the project should go forward with: [ 

1155 

In the December 1990 monthly report, Kawamura reported the results of her continued preliminary 

147 RFF 1.139 (no dispute). 

14’ SFF 113 (no dispute). 

149 SFF 114 (no dispute). 

I5O SFF 115 (no dispute). 

15’ RFF 1.141 (no dispute). 

152 RFF 1.149 (no dispute). 

153 Kojima, Tr. at 387. 

154 Id. at 398-99. 

155 SFF 130 (no dispute); see also JX-1 1CT at AHL430884. 

38 
experimentation on the above enumerated strains. Additionally, Kawamura stated that she had 

obtained [ ] Of those 150, the top three 

lysine producers were No. 70 at [ ]No. 11 at [ ] andNo. 61 at [ 1156 

In December 1990, Kawamura derived AE-70 [ Although the AE-70 strain 

did not yet include the specific mutations to the dapA gene claimed in the ‘160 patent, in the May 

1992 monthly report, Kawamura reported that the AE-70 strain was the “best Lys producer strain . 

. . so far.”158 In the same monthly report, Kawamura, Ogawa and Sano, reported that AE-70 was a 

“very important” intermediate strain for development. 159 Because of its importance, the researchers 

initiated investigation of the [ ] of this strain.’60 

In June 1992, Kawamura investigated the [ ] of the AE-70 strain. In the June 

1992 monthly report, Kawamura reported that the AE-70 strain, which Kawamura again characterized 

as the “best Lys-producing bacterium,”was[ ] conditions tested.161 

Kawamura also reported that the lysine yield for AE-70 was [ ]I6* In the same report, Kawamura, 

Ogawa and Sano, concluded that the [ 3 of the AE-70 strain was t01erable.I~~ Additionally, 

Kawamura reported that she had derived from the [ ] two new 

156 SFF 133 (no dispute); see also JX-12CT at AHL430878. Kawamura also reported that 

according to TLC one strain derived from W3 1 10 allegedly had lysine producing activity. However, 

Kawamura noted that a lys peak was not detected with liquid chromatography and therefore the TLC 

spot was not from lysine. Id. 

157 

158 

159 

160 

161 

162 

163 

RFF 2.58 (no dispute). 

JX-83 CT at AHL43 0 804. 

Id. at AHL430803. 

ld. 

JX-84CT at AHL430801. 

Id. 

Id. at AHL430800. 

39 
strains: BA-329 and BA-339.’64 According to the June 1992 monthly report, the lysine yield from the 

AE-70 strain [ 3 was greater than the yield from the two new strains [ 1 and[ 1 

In the July 1992 monthly report, Kawamura reported that “[tlhe best lysine producer E.coli 

strain is AE-70, the strain developed from [ 

Kawamura also reported that “[tlhe second best strain is BA329 developed from [ 

According to Kawamura, the AE-70 strain showed some [ 

In 

contrast, Kawamura reported that “in BA329, a marked [ 

Both Kawamura and Sano noted in the July 1992 monthly 

report that there was a loss of [ 3 in AE-70, but reported that the degree of loss was 

still acceptable to consider the study results useful.’70 On the other hand, with regard to strains 

BA329 and BA339, Kawamura and Sano reported that the productivity of those strains declined from 

[ ]to[ ] and from [ ] to almost[ ] respe~tive1y.l~’ Thus, the decrease in productivity in 

the AE-70 strain was less than the decrease observed in the competing BA329 and BA339 strains.’72 

In the August 1992 monthly report, Kawamura reported the results of her research on the 

[ 3 in the AE-70 strain and found that the AE-70 strain showed good 

Id. at AHL430801. 

JX-85CT at AHL430799. 

165 Id. 

167 Id. 

16* Id. 

169 Id. 

17’ Id. 

17* See JX-85CT. 

Id. at AHL430798. 

40 
[ ] in both of the tests she ran.173 In the same report, Kawamura and Sano concluded that AE70 was “[ 1331~~ 

In the September 1992 monthly report, Kawamura reported the results she obtained when she 

recultured certain AE-70 transformants with genes for lysine bio~ynthesis.’~~ Kawamura also reported 

that the genes for lysine biosynthesis had been introduced into the BA329 strain.176 Specifically, 

Kawamura noted that the same four types of clones [ 3 that 

showed [ ] were introduced into the BA329 strain.177 Kawamura 

reported that the introduction of the dapA24 gene, which increased lysine yield the most in AE-70, 

was rather inhibitory in the BA329 strain.17’ According to Kawamura, “[m]ore cadaverine and less 

Lys were produced compared to AE-70.”179 This led Kawamura and Sano to conclude that BA329 

was “inferior” to AE-70.I8’ Accordingly, Kawamura and Sano decided to [ 

] the strain from which BA329 was derived.181 

In the October 1992 monthly report, Kawamura and Sano reported their decision to focus on 

the current AE-70 strain. Kawamura and Sano also reaffirmed that[ 

]I8’ Additionally, Kawamura and Sano 

reported plans to produce further changes and improve characteristics of the AE-70 strain, and to 

173 JX-86CT at AHL430797. 

174 Id. at AHL430796. 

175 JX-87CT at AHL430795. 

176 Id. 

177 

178 Id. at AHL430795. 

179 Id. 

Id. at AHL430794. 

Id. 

JX-89CT at AHL430793. 

Id.; see aZso id. at AHL430794 (Kawamura and Sano stated that the four clones 

“increased productivity greatly in AE-70.”). 

41 
cultivate an [ iiS3 

In the November 1992 monthly report, Kawamura and Sano reported that they had 

“discovered clones among lysC* and dapA* clones that increased the lysine productivity of AE-70, 

but [ The inventors noted that next month they would again pursue efforts 

including use of competent cells properly prepared and strains with [ 

Kawamura and Sano also reported that they planned to grow [ 

iiS5 

In the December 1992 monthly report, Kawamura reported on her efforts to investigate why 

]Is7 Kawamura surmised based on her investigation 

]Is8 In the same 

AE-70 had previously shown [ 

that the reduction in lysine production was caused by a [ 

report both Kawamura and Sano reported that “[tlhe strongest existing lysine bacteria, AE-70, has 

recently undergone a drastic titer reduction, . . . but, as seen on the attachment, when [AEC] was 

actually used, [I vast improvement was observed, I 1,’189 Kawamura 

also reported in December that she reintroduced the [ 

According to Kawamura, the results of the introduction 

were remarkable, attaining a maximum yield of [ ] and an average yield of [ Sano 

confirmed these results in the same report, stating “[tlhe result is absolute best: we achieved max 

Id. 

JX-90CT at AHL430791. 

Id. 

lS6 Id. 

lS7 JX-91CT at AHL430790. 

Id. 

Id. at AHL430789 (emphasis in original). 

AE-70f was the strain obtained by reselecting AE-70 wth AEC. RFF 2.105 (no dispute). 

191 Id. at AHL430790. 

19* Id. 

42 
[ Kawamura did note that there were numerous reductions in titer during recultivation, but that there were four strains that had favorable res~1ts.l~~ On this point Sano reported 

that “[ulpon re-cultivating the transformant, . . . [ 3 was the result. As the 

other clones were also [ ] or higher, at 100% survival titer, the results were ac~eptable.”’~~ 

In the January 1993 monthly report, Kawamura reported that the plasmid carrying the 

dapA*24 mutation was [ 

The resulting mutant was referred to as pMWdapA*24 and is the same dapA 

mutant described in the ‘ 160 patent at issue in this in~estigati0n.l~~ Kawamura reported that the AE70 strain with the pMWdapA*24 mutant had a maximum yield of [ 1 as 

compared to the AE-70 strain without the mutant, which had a yield of [ Kawamura reported 

that the strain that achieved the maximum yield of [ 3 lysine in a 48 hour period 

with residual sugar.199 Sano confirmed these results in the same report and additionally noted that 

“[ilf the productivity is [ 3 then we will use it as the base strain for future experiments, such as 

for gene combination.”200 

] produced [ 

In the February 1993 monthly report, Kawamura reported on the [ 3 she 

performed on the transformant strain of AE-70/pMWdapA*24 discussed in the January 1993 monthly 

. 

193 Id. at AHL430789 (emphasis in original). 

194 Id. at AHL430790. 

195 Id. at AHL430789. 

196 JX-92CT at AHL430788; see aZso RFF 2.109 (no dispute). 

197 RFF 2.1 10 (no dispute). 

19* JX-92CT at AHL430788. 

199 Id. 

2oo Id. at AHL430787. 

43 
report.2o1 Kawamrua reported that the test showed an almost [ ] reduction in yield than that 

previously cultivated with a maximum yield of [ ] and an average yield of [ I2O2 The 

plasmids, however, [ 

confirmed that [ 

a maximum yield of [ 

1203 In the same report, Sano 

3 and 

Sano also confirmed that the plasma retention rate was almost 

] were approximately [ 3 with an average yield of [ 

I2O4 

Sano also noted that [ 3 significantly rose.2o6 

In the March 1993 monthly report, Kawamura reported on efforts to optimize the culturing 

conditions of AE-70 as well as the results of introducing both the dapA* mutant and lysC* mutant 

to the AE-70 strain.207 Kawamura noted in the report that AE-70 was currently the only lysine 

producing strain.208 Kawamura also reiterated that the introduction of dapA* [ ] (i. e., 

pMWdapA*24) to AE-70 enhanced lysine production capability by In the same report, Sano 

noted that lysine production by AE-70, including recombinant strains, was somewhat [ I2l0 

Sano hypothesized that the reason for the[ 

Sano reported the results of efforts to optimize the culturing conditions, stating: 

3 was due to inappropriate culturing conditions.211 

1 

201 JX-93CT at AHL430786. 

202 Id. 

203 Id. 

204 Id. at AHL430785. , 

205 Id. 

206 Id. 

207 JX-94CT at AHL430784. 

208 Id. 

209 Id. 

210 Id. at AHL430783. 

211 Id. 

44 
Sano also reported on the results obtained when both the dapA* mutant and lysC* mutant were 

introduced into the AE-70 strain.213 According to Sano there was a slight improvement, from a yield 

of [ 3 with the [ ] to a yield of [ ] with the [ 

I2l4 Sano also noted that [ ] showed complete 

[ ] of the pMWdapA*24 mutant while the plysC*43 mutant showed[ i215 

Research Report No. 4 reports on research performed between April 1992 and March 1993. 

Kawamura and Sano were co-authors of the report, and Kawamura presented the report internally.216 

The Ajinomoto researchers noted in the report that the “AE-70 strain was superior in lysine 

production capacity” and showed good [ ] under certain conditions.217 The researchers 

also noted in the research report that they had derived strains from [ ] but that “a strain 

superior to the AE-70 strain was not obtained.”218 

Research Report No. 5 covered research performed between April 1992 and March 1993 .219 

In the report, Sano and Kawamura noted that when the mutant dapA gene was loaded onto a [ 

3 that was introduced into AE-70, “there was an effect on the lysine productivity, but it was 

] mutant dapA [ In addition to reporting on transformation of AE-70 with a [ 

212 

213 

214 

215 

216 

217 

218 

219 

220 

Id. 

Id. 

Id. 

Id. 

RFF 2.135 (no dispute). 

JX-127CT at AHL435972, AHL435993. 

Id. at AHL435974. 

RFF 2.144 (no dispute). 

JX-95CT at AHL003062. 

45 
plasmid, Sano and Kawamura also reported on the transformation of AE-70 with [ 3 

mutant dapA plasmids.221 The results of the reproducibility tests set forth in the fifth research report 

showed that yields of the AE-70 strains ranged from [ 

c 3 during the retest.222 

3 in the first tests and ranged from 

In the April 1993 monthly report, Ogawa reported that AE-70 used as an E.coli lysine 

producing host yields [ ]223 Ogawa also reported that 

introduction of the mutant dapA by plasmid increased production to approximately [ ]224 In the 

same report, Kawamura noted that the AE-70 strain derived from [ 3 was the best microbe for 

E.coli lysine production.225 Kawamura also reported that an AEC-resistant strain had been collected 

from [ 3 (i. e., BA329), but noted that lysine decomposition was observed.226 Additionally, 

Kawamura reported that there was a plan to elaborate the mutation and derive a better lysine 

3 lysine relative to [ 

producing microbe, and to re-obtain and evaluate several AEC-resistant strains from [ 1227 

In the May 1993 monthly report, Ogawa reported that she had prepared a variety of types of 

dapA plasmids.228 Ogawa reported that next month, “these plasmids will be introduced to AE-70, the 

current host for E.coli lysine-producing microbe.”229 In the same report, Kawamura noted that 

because the best E.coli lysine producing microbe obtained (i. e., AE-70) was a threonine-producing 

strain with AEC resistance, the decision was made “[ 1 

221 RFF 2.150 (no dispute). 

222 JX-95 at AHL003066. 

223 JX-38CT at AHL430781. 

224 Id. 

225 Id. at AHL430782. 

226 Id. 

227 Id. ; see also id. at AHL430779. 

228 JX-39CT at AHL430777. 

229 Id. 

46 
[ 

microbe, and clarify the mutation of the AEC-resistant strain.”230 

3 to obtain [an] even better Lys-producing 

In the June 1993 monthly report, Ogawa reported the effects of the introduction of sixteen 

various dapA plasmids on the “E.coli lysine-producing microbe host AE-70.”231 Ogawa reported that 

among vectors with [ ] there were discrepancies in production, but that among 

vectors with [ ] reproducible results were obtained for eight varieties.232 Ogawa also 

reported that even among wild types, the effect of the introduction of the dapA plasmids corresponded 

to the number of copies and that in the inhibition-release type, results were further improved.233 

According to Ogawa, lysine production from the AE-70 strains with the RSF24P and pMW24P 

plasmids was the highest with a yield that was approximately 2.5 times that of AE-70 without the 

addition of a dapA plasmid.234 In the same report, Kawamura reported on her efforts to breed a lysine 

producing microbe from an AEC resistant [ 3 strain.235 The report states that lysine production 

capability was investigated in 500 AEC resistant strains derived from [ ]236 Kawamura reported 

that the highest lysine accumulation was [ 3 which was still not the desired accumulation, and 

thus derivation of an AEC resistant strain was abandoned.237 

In the July 1993 monthly report, Ogawa reported that culturing showed that the lysine 

230 Id. at AHL430778. 

231 JX40CT at AHL430773. 

232 Id. 

233 Id. 

234 Id. 

235 Id. at AHL430774. 

236 Id. 

237 Id. 

47 
producing capabilities of AE-70 were lower than that previously obtained.238 Ogawa surmised that 

the [ 3 and thus it was determined to 

eliminate this using P1 phage.239 After obtaining 24 strains that did not require [ ] and that were 

AEC resistant, new testing was done.240 The results of the testing showed that only one strain fully 

recovered, AE-70[ ] were the same as AE70.241 According to Ogawa, that strain was to be used as the lysine producing bacterium host 

beginning next month.242 In the same report, Kawamura reported on the results of the introduction 

of the pMWdapA*24 plasmid into the AEC resistant strains of [ 3 obtained last month.243 

Kawamura reported that an increase in lysine production was seen in virtually all of the strains, but 

that the increase in production did not reach the level “attained with the dap introduced strains in the 

current lys-producing bacterium AE-70 [ Noting that “AE-70 is the 

bacterium having the highest lys production of the AEC resistant bacteria obtained thus far,” 

Kawamura also reported on her efforts to [ 

3 was due to the fact that the bacteria required [ 

and that its growth and lysine producing ability [ 

]245 Based on the results obtained, Kawamura 

concluded that there was at least one AE-70 mutation other than the AEC resistance mutation, and 

that this unknown mutation appeared to be essential to high lysine production.246 On this point, 

Kojima wrote in the same report that “AEC resistance mutation was introduced to both [ 1 and 

238 JX-41CT at AHL430766. 

239 Id. 

240 Id. 

241 Id. 

242 Id. 

243 Id. at AHL430768. 

244 Id. 

245 Id. 

246 Id. 

48 
[ 3 but Lys producing capability was between [ 3 and [ 3 which was considerably lower 

than AE-70.”247 

In the August 1993 monthly report, Ogawa reiterated that in order to resolve issues of 

3 requirement was eliminated from the strain.248 This new strain was 

with AE-70, 

In the same report, 

[ 

designated AE-70[ 

ultimately concluding that AE-70 would continue to be used as the 

Kawamura reported on her work with the [ 

] with AE-70, the [ 

3 Ogawa reported on the results of tests comparing AE-70[ 

3 strain.250 Kawamura reported that [ 

3 and then the dapA plasmid was intr~duced.~~’ 

3 probably due to a 

]252 Kojima also noted in the same report that work was being performed 

Kawamura reported that [ 

[ 

to try and solve AEC-resistant mutation issues with AE-70.253 

3 resulted in a [ 

In the September 1993 monthly report, Kojima reported on efforts to investigate the mutation 

points of ~~-70.~~~ Kojima reported that screening for strains using lys-auxotrophy bacteria (E.coli) 

as an index was unsuccessful and that screening would be rerun using AEC resistance as an index.255 

In the same report, Ogawa reported on work with the AE-70 strain transformed with the dapA* and 

lysC* plasmids.256 Ogawa reported that [ 3 rose approximately [ 3 

247 Id. at AHL430765. 

248 JX-42CT at AHL430761. 

249 Id. 

250 Id. at AHL430762. 

251 Id. 

252 Id. 

253 Id. at AHL430759. 

254 JX-209C at AHL430754. 

255 Id. 

256 Id. at AHL430755. 

49 
due to the dapA and lysC Also in the same report, Kawamura reported on the results 

of introducing dapA and lysC into AEC-resistant strains of [ 1258 

According to Kawamura [ 

reported on efforts to introduce dapA and lysC into AEC-resistant strains of [ 

] showed no effect on Lys production.259 Kawamura also 

Kawamura noted that when compared to dapA alone, the introduction 

of both dapA and lysC led to better results with a maximum of [ ] Lys and ] Thr seen after [ 

colony separation.261 In a separate monthly report from September 1993, Kikuchi noted that 

“[c]wently, strain [ ]Thr-producing bacteria are used as hosts for GE-E.coli Lysproducing bacteria. Therefore, as a different approach, it has been thought to construct Lys-producing 

bacteria hosts with strains other than Thr-producing bacteria.”262 To test this new approach, various 

strains were created from wild-type W3 1 10, including a W3 1 10 (tyrA) strain and a W3 1 1 O(tyrA,tyrR) 

strain.263 The testing showed that the tyrR and tyrA deficient strain of W3 1 10 transformed with the 

] and strain [ 

RSFDSO plasmid produced the highest results with [ 3 lysine and a yield of [ 1264 

In the October 1993 monthly report, Kojima reported that he had decided to submit the dapA* 

and dapA* + lysC* in one patent application and was in the process of preparing the specification and 

bacterial strain for deposit.265 Kojima also reported that “[wlhen [ 

3 into AE-70, yield did not change, but growth became [ 1 

257 Id. 

258 Id. at AHL430756. 

259 Id. 

260 Id. 

26’ Id. 

262 JX-2 1 CT at AHL430737. 

263 Id. 

264 Id. 

265 JX-44CT at AHL430747. 

50 
times during B.O.). Will introduce RSFD80 (dapA* + lysC*) and further cultivate (Continued by 

Nishimura).”266 In the same report, Kikuchi summarized his efforts to breed a lysine producing 

bacterial host from strain W31 Also in the same report, Ogawa reported on her efforts to 

improve growth characteristics.268 Specifically, Ogawa reported that for strain RSFD80/AE-70, 

growth worsened under current culture conditions, with a residual glucose of 1/5 with 48-hour flask 

cultivation, and a tendency for OD to drop in the latter half of cultivation.269 Ogawa hypothesized that 

the drop in OD was due to a lack in substances needed for growth and thus performed six types of 

additional cultivation for the three types of required amino acids [ 3 as well as [ 

]270 According to Ogawa, the results showed an improvement in growth with the 

] with a residual glucose of [ ]271 However, although yield dropped with 

] and yield both improved about [ ]272 Ogawa noted that he planned 

] by modifling the media.273 In a separate report from 

addition of [ 

addition of [ 

to continue his efforts to [ 

October 1993, researcher Nishimurareported the results of tests on AE-70 with [ 3 (“AE70L”).274 Nishimura reported that strain AE-70L/RSFD80 showed an accumulation of [ 1 and 

a[ 

also reported that AE-7OLDZSFD80 consumed [ 

] yield, which was [ ] better than the yield achieved with AE-70/RSFD80.275 Nishimura 

] of the initial sugar after a 46-hour culture and 

266 Id. 

267 Id. at AHL430748. 

268 Id. 

269 Id. 

270 Id. 

271 Id. 

272 Id. 

273 Id. 

274 JX-198CT at AHL500025. 

275 Id. 

51 
also increased the sugar consumption rate compared with AE-70RSFD80 that left [ 

sugar.276 

3 of 

In Research Report No. 6, which covers April 1993 - October 1993, Ogawa reported that the 

host bacteria with the highest yield was AE-70 (AJ12609) with a yield of [ ]277 However, 

when dapA, and lysC genes were introduced to AE-70 using plasmids, Ogawa reported that yield 

improved more than While yield improved more than twice, Ogawa reported that the lysine 

production ability of the strain was [ 3 and thus it was necessary to devise an optimization of 

the [ 3 of both genes and [ 1279 

In the November 1993 monthly report, Kojima noted that the dapA* and dapA* + lysC* 

patent application was being prepared and that he planned to apply for the patent in December at the 

latest.280 In the same report, Ogawa reported that he had performed lysine added cultivation to 

examine whether RSFD80/AE-70 maintains its ability to produce lysine under [ 1 

conditions.2s' Ogawa observed that yield was the same as with the control group when [ 

3 was added, but when [ 3 were 

added "slight drops were observed [ Ogawa hypothesized that the slight drop was due 

to an increase in [ ]283 In a separate report from November 1993, Nishimura reported 

that he obtained a yield of [ 3 when the RSFD80 plasmid was introduced into the [ 

276 Id. 

277 JX-45 at AHL003086. 

278 Id. 

279 Id. 

2so JX- 12 1 at AHL43074 1. 

281 Id. at AHL430742. 

282 Id. 

283 Id. 

52 
3 strain.284 In yet another separate report from November 1993, J. Kojima 

reported that he had cultured AE-7O/RSFDSO in an S-jar, but found that [ 3 suddenly declined and 

growth stopped in about 12 J.Kojima noted, however, that the likely cause was simply an 

insufficient amount of nutrients in the S-jar.286 More particularly, J.Kojima hypothesized that the 

cause was a lack of [ ]287 

Research Report No. 9, presented by Kawamura covered research performed between April 

1993 and March 1 994.288 In the report, the researchers reitterate that “[iln the process of breeding 

lysine producing bacteria, it goes without saying that an excellent host is necessary.”289 Kojima and 

Kawamura also wrote that AE-70 had “the highest yield among the bacterial strains obtained until 

present .”290 

The December 1993 monthly report is dated December 22,1993, which is after the December 

8,1993 filing date of the Japanese priority patent appli~ation.~~’ While undoubtedly the research that 

is reported in this monthly report occurred before its December 22, 1993 date, it is entirely unclear 

what specific research was conducted, and thus known to the inventors, prior to December 8, 1993. 

Moreover, December 8, 1993 is the date the patent application was filed, which implies that the 

application was written sometime earlier. In fact, in both the monthly reports for October 1993 and 

November 1993, Kojima explicitly notes that he was preparing the patent applications during that 

284 JX-199CT at AHL500024. 

285 JX-200CT at AHL500035. 

286 Id. 

287 Id. 

288 RFF 2.21 8 (no dispute). 

289 JX-96CT at AHL436045. 

290 Id. 

291 See JX-60CT. 

53 
time. Thus, the undersigned gives little weight to the research results reported in the December 1993 

monthly report in determining the inventors’ subjective preference as of the filing date of the Japanese 

priority patent on December 8, 1993. 

As detailed above in the monthly and research reports, the documentary evidence of record 

clearly shows that from the outset of the Lysine Project in 1990 to the filing of the Japanese priority 

patent application in December 1993, the inventors and researchers on the project had a preference 

for AE-70 as the host strain. While the undersigned is mindful that the focus of the best mode 

analysis is on the inventors’ subjective intent at the time of filing, the inventors’ views regarding AE70 during the period from October 1990 through the filing of the Japanese priority patent application 

in December 1993 are undoubtedly relevant to that determination. Here the remarks made in the 

monthly and research reports show a pattern of preference favoring AE-70 over the other strains the 

researchers were examining. Throughout the relevant period, AE-70 was consistently referred to in 

the reports as the “best” lysine producing strain. The inventors’ use of the word “best” to describe 

AE-70 inherently connotes a subjective preference for that host strain. Additionally, in at least two 

instances where the AE-70 strain was compared to a B-3996 strain, the inventors explicitly referred 

to the B-3996 strain as “second best” and “inferior to AE-70,” thereby affirming their preference of 

AE-70 over B-3996.292 That is not to say that AE-70 was perfect. To the contrary, the documentary 

evidence shows that the researchers had issues with AE-70, as they did with all of the strains they 

were working with. However, as opposed to the other strains the researchers were investigating, the 

documentary evidence shows that in practically every instance, AE-70 was the better performer; vis., 

292 See JX-85CT at AHL430799; JX-87CT at AHL430794; see also JX-127CT at 

AHL435972; JX-41CT at AHL430768. 

54 
more stable, better accumulation, higher yield. With regard to accumulation in particular, the 

documentary evidence shows that AE-70 was the best lysine producing host strain the researchers had 

created. Specifically, in October 1993 the researchers reported that they had transformed AE-70L [ 

3 with the RSFD80 plasmid (plasmid having both mutated dapA 

and lysC ) and had achieved [ 3 lysine. Notably, grams per liter is the only measurement of 

lysine production used in Tables 5-7 of the specification of the ‘ 160 patent to illustrate the invention 

of claim 1 5.293 In contrast to the [ 3 lysine produced using AE-70LRSFD80, the highest 

producing lysine strain disclosed in Tables 5-7 was W3 1 1 ORSFD80, which produced only [ 3 

As previously discussed, Ajinomoto argues that the inventors did not have a subjective 

preference for the AE-70 strain. In support, Ajinomoto relies on Kojima’s testimony explaining why 

he did not consider the AE-70 host strain to be the best host strain at the time of the priority 

application. However, with regard to Kojima’s testimony on this point, the undersigned notes that 

Kojima testified as follows: 

293 Under the heading “Best Mode For Carrying Out The Invention” in the specification of 

the ‘ 160 patent, the inventors disclose a number of examples. Only Examples 1-5, which include 

Tables 5-7, are pertinent to the best mode analysis of claim 15 of the ‘160 patent. The other 

examples and tables in this section were added later in time in the PCT application and relate to the 

subject matter of other non-asserted claims. See CRRFF 1.66-1. 

With regard to the fact that grams per liter is the only measurement of lysine production 

used in Tables 5-7, the undersigned notes that that during prosecution the applicants relied upon 

the information set forth in Tables 1,5,6 and 10 of the specification in support of their arguments 

for patentability. See, e.g., JX-112 at AAHL001440 (Table lo), AAHLOO1441 (Tables 5-6), 

AAHL001502 (Table 1). In fact, the applicants relied upon the “high” yield in an effort to 

overcome a rejection. Id. at AAHL001503 (“The L-lysine concentration (0.18mM = O.O26g/L, 

pBT5 17) produced in the culture supernatants as disclosed in Table 1 of the reference is much 

lower as compared to the lysine concentrations produced by the transformed bacteria as disclosed 

in the present specification, for example, 9.17 g/L (see Table 10 at page 88 of the present 

specification). These high levels of L-lysine production by the transformed Escherichia bacteria 

would not be expected from Falco et al.”) (emphasis added). 

55 
. Q. Dr. Kojima, isn’t it true that you don’t recall why you did not disclose the results 

that you and your team members obtained with AE-70 in the ‘1 60 patent? 

A. With regards to this matter, I have looked at many monthly reports and researcher 

reports, and I have had a conversation with very many people. And at this point in 

time, I just cannot differentiate in my mind as to what I was thinking back then, and 

what opinion and understanding I have come to hold . . . concerning this issue.294 

Kojima’s admission that he could not differentiate between his present opinion regarding the reason 

AE-70 was not disclosed and his opinion at the time of filing the Japanese priority patent application 

renders his opinion testimony unreliable, because the best mode inquiry is focused on an inventor’s 

subjective preference at the time of filing and not any later formed opinion. This includes Kojima’s 

testimony explaining his subjective preference for the various host strains disclosed in the ‘ 160 patent 

and his testimony regarding why he felt the AE-70 strain was not the best mode for carrying out the 

invention. In these matters the undersigned gives no weight to Kojima’s testimony at the hearing. 

Ajinomoto relies in support of its contention that the inventors did not have a subjective 

preference for the AE-70. strain on testimony, primarily from Kojima, that the inventors had issues 

with AE-70 relating to its [ 

]295 Examples of Ajinomoto’s treatment of the evidence regarding AE-70’s alleged 

deficiencies are set forth below. 

With regard to [ 3 Ajinomoto asserts, citing the July 1993 monthly report, that the 

“inventors and their colleagues encountered ongoing problems of [ 

] when testing AE-70 that contained the patented mutations.”296 However, each of the metrics 

compared in the July 1993 report shows that AE-70 was superior to the derivatives of [ ] which 

294 Kojima, Tr. 480:12-25. 

295 CIB at 22-23. 

296 CFF 5.52. 

56 
were also tested.297 Ajinomoto also asserts, citing a July 1992 monthly report, that “[elven prior to 

being transformed with any genetic modifications, the AE-70 strain showed signs of [ 3 but 

was still useful for study.”298 However, Ajinomoto fails to point out that in the same report the 

researchers noted that the two strains derived from [ 3 which were subjected to the same [ 1 

conditions, showed signs of greater [ ]299 Ajinomoto further asserts, citing a research report 

covering the period from April 1992 to March 1993, that AE-70’s high yield performance was not 

maintained after [ ] thereby casting doubt on AE-70’s ~tility.~” However, the 

same research report indicates that the [ 3 issues were largely settled.301 

With regard to growth rate, Ajinomoto asserts that in March 1993, the researchers were 

studying ways to optimize the culturing conditions of AE-70, and that by October 1993, “the 

inventors could not get the AE-70 to grow: ‘RSFDSO/AE-70, growth worsens under current culture 

conditions. . . .”’302 However, in a separate monthly report from October 1993, Dr. Nishimura stated: 

[ 

1303 

297 See JX-41CT. 

298 CFF 5.53. 

299 See JX-85CT. 

300 CFF 5.55. 

301 See JX-127CT at f 3-4 (“The lysine production of these colonies is as shown in Fig. 13, 

302 CFF 5.66. 

303 CX-198 at AHL437298. 

showing that more stable storage is possible through use of a minimal medium.”). 

57 
Ajinomoto also asserts, based on the November 1993 monthly report, that an S-jar experiment 

showed that yield for AE-70 was approximately half of the yield in a flask and that growth of AE-70 

stopped in 12 hours. On this point Kojima testified that “[tlo see how bad the problem was, we tested 

the strain in a larger container called an S-Jar in November 1993, our Dr. J. Kojima reported AE-70 

with RSFDSO plasmid grew poorly in the fermentor. Not only was growth poor, but the previously 

‘best’ lysine yield numbers observed in a laboratory flask were not reproduced.”304 However, 

Ajinomoto fails to point out that in the same November 1993 report, the researchers state that the 

cause for the slow growth followed by its eventual cessation was insufficient nutrients in the medium. 

Specifically, the November 1993 report states, “[wle assumed that some substrates had run out we 

found that [ ] ran out - examine 

[ ] amount.”3o5 

] was missing based on TLC. It is therefore most likely that [ 

With regard to sugar consumption, Ajinomoto asserts: (1) based on the research report 

covering April 1993 through October 1993, that for AE-70RSFD80 “the residual sugar is 

approximately 114 with 48-hour cultivation and the growth and sugar consumption rates are very 

slow;” (2) based on the research report covering September 1993 through May 1994, that AE70RSFD80 had “a problem in that the growth for this strain was too slow, and unable to consume 

40 g/1 glucose in a 48-hour flask culture;” (3) based on the research report covering April 1993 

through March 1994, that AE-70 had “high yield, low growth and sugar consumption ability, and 

cannot utilize sucrose;” and (4) based on the research report covering December 1993 through March 

1994, that “although this strain has high lysine yields, it has problems of [ 1 

304 CFF 5.71; CFF 5.72. 

305 See JX-200CT. 

58 
Although Ajinomoto cites to four sources in support of its finding, a 

review of the underlying research reports shows that each of the first three reports describes the results 

from a single test and the fourth merely sumarizes those results.307 Ajinomoto also asserts based on 

the October 1993 monthly report that AE-70RSFD80 with dapA & lysC showed[ 1 of 

approximately [ 

Dr. Nishimura found that by using AE-70RSFD80 with [ 

I3O8 However, as discussed above, in a separate October 1993 monthly report, 

] he was able to obtain results 

where “[tlhis strain consumed 40 g/L of initial sugar after 46-hour culture and also increased the sugar 

consumption rate compared with AE-70RSFD80 that left [ ] of sugar.”3o9 

With regard to reproducibility, Ajinomoto asserts that the [ 3 of AE-70 disqualified 

the strain from being used to best demonstrate the effect of the dapA m~tation.~” However, while 

AE-70 may have had some issues with [ 3 the evidence of record demonstrates that AE-70 

was generally more [ ] than any of the other strains with which Ajinomoto was working. 

Notably, in the July 1992 monthly report, experiments comparing the [ 3 of AE-70 

versus derivatives of [ ] showed that the loss in producibility by AE-70 was acceptable, but the 

losses in the derivatives were so bad that the researchers suspended their work on those strain^.^" 

With regard to [ 3 Ajinomoto asserts based on the research report covering 

the period from November 1993 through March 1994, that prior to the filing of the Japanese priority 

patent application, the researchers learned that “inhibition in the lysine production [of AE-701 was 

t 

306 CFF 5.78. 

307 See JX-45CT; JX-52CT; JX-96CT; JX-250CT. 

308 CFF 5.95. 

309 See JX-198CT. 

310 CFF 5.103. 

311 See JX-85CT. 

59 
not based on the [ On this 

point, Kojima testified that “[mly recollection is that this data [Figure 3-5-71 was obtained prior to 

the Japan filing date . . . in late November 1993.”313 Contrary to Ajinomoto assertion, however, the 

evidence of record indicates that the comparison [ ] test on which Ajinomoto relies 

could not have been run prior to the December 8, 1993, filing of the Japanese priority patent 

application. Specifically, the research report provides results of [ 3 testing on the 

following strains: AE-70, WC80, BDL215, and TA-325.314 However, the evidence of record shows 

that the TA-325 strain was not created until approximately January 1994.315 Additionally, the 

3 but due to the [ 

evidence of record indicates that decreases in yield of lysine with increases in [ 1 appear 

to be accociated with all E.co1i strains.316 Further, the evidence of record shows that the AE-70 strain 

fared better than any of its competitors in these comparison tests. Specifically, the report noted: 

[ 

1 

312 CFF 5.1 13. 

313 Id. 

314 See JX-98CT at AHL436060. 

315 See Kojima, Tr. at 560; JX-96 at AHL436044. 

316 See JX-98CT at AHL436081 (“Generally, E.coli has been known to be more sensitive to 

[ ] compared to brev.”). 

60 
Thus, according to the report, while lysine production by derivatives of [ ] decreased 

dramatically (down to zero in certain instances), the lysine production by the AE-70 strain only 

decreased slightly under the high [ i318 

As shown above, Ajinomoto’s arguments are often highly selective, focusing on every 

criticism in the monthly and research reports to the exclusion of other more favorable comments made 

about AE-70 in the very same reports.319 Additionally, Ajinomoto conflates its argument by relying 

on the same tests in the same reports to allegedly show a whole plethora of deficiencies in the AE-70 

strain. The undersigned finds the evidence on which Ajinomoto relies does not overcome the clear 

and convincing documentary evidence discussed in detail, supra, that shows that the inventors had 

a subjective preference for AE-70. Moreover, whatever issues the inventors had with AE-70, the 

documentary evidence shows that AE-70 was still Ajinomoto’s best strain, regardless of the metric 

used, and the one the inventors preferred at the time they made their priority application. 

Accordingly, for the reasons set forth hereinabove, the undersigned finds based on the 

documentary evidence of record that the inventors of the ‘ 160 patent had a subjective preference for 

the AE-70 host strain at the time of filing the Japanese priority patent on December 8, 1993. 

Having determined that the inventors had a subjective preference for the AE-70 host strain 

at the time of filing the Japanese priority application, the best mode analysis turns to the second 

317 JX-98 at AHL436082-83. 

318 Id. 

319 It is somewhat ironic that while Ajinomoto accuses GBT and the Staff of “cherrypicking” from the monthly and research reports to support their contention that the inventors of the 

‘160 patent had a preference for the AE-70 host strain, it is in fact Ajinomoto that is guilty of 

“cherry-picking” from the reports. 

61 
inquiry, which asks whether the inventors’ disclosure is adequate to enable one of ordinary skill in 

the art to practice the best mode of the invention. As previously discussed, this second inquiry is 

objective and depends on the scope of the claimed invention and the level of skill in the relevant art. 

Ajinomoto argues that GBT failed to show an objective violation, because there is no evidence 

that the specification of the ‘ 160 patent fails to enable one of ordinary skill in the art to practice the 

best mode of the claimed invention. Ajinomoto’s argument is premised on its belief that the scope 

of the claimed invention is limited to the specific mutations to the dapA gene. However, the 

undersigned has previously found this argument to be in error and has held that the scope of the 

claimed invention includes the production of lysine by a host strain from the genus Escherichia 

transformed with the specific dapA mutant, as well as, the accumulation and cultivation of the lysine. 

Because the scope of the claimed invention encompasses the host strain and the evidence shows that 

the inventors had a subjective preference for the AE-70 host strain at the time of filing the Japanese 

priority patent application, the inventors were obligated under Section 1 12 to disclose that preference. 

There can be no question that the AE-70 strain was not disclosed in the ‘160 patent.320 Thus, the 

undersigned finds the ‘ 160 patent disclosure insufficient to enable one of ordinary skill in the art to 

practice the inventors’ preferred embodiment of the invention as claimed in claim 15 of the ‘ 160 

patent, vis., the AE-70 host strain transformed with the dapA mutant. 

For the reasons discussed herein, the undersigned finds that Ajinomoto’s concealment of its 

preferred embodiment of claim 15 of the ‘ 160 patent to be a violation of the best mode requirement. 

Accordingly, the undersigned finds claim 15 of the ‘ 160 patent invalid under 35 U.S.C 0 1 12.321 

320 See JX-1. 

321 Ajinomoto argues for the first time in its post-hearing brief that even if the undersigned 

(continued.. .) 

62 
b. The disclosed best mode was fictitious 

GBT argues that the inventors did not actually perform the lysine-production experiments 

described in the ‘160 patent with the disclosed strains and thus the examples in the patent are 

fictitious and invalid under 35 U.S.C. 0 1 12.322 Specifically, GBT argues that the inventors did not 

perform the disclosed experiments with strains B-399 and W3 1 lO(tyrA) as described in Examples 

3-5 and set forth in Table 5-7.323 With regard to strain W3 1 1 O(tyrA), GBT argues that Kojima admits 

that the inventors did not actually use W31 GBT also argues that Kojima’s attempt to 

characterize strain W3 1 lO(tyrA) as merely an abbreviation for the actual strain the inventors used 

should not be credited given the detailed description of how the W3 1 1 O(tyrA) strain was derived in 

the ‘160 patent.325 GBT asserts that Ajinomoto’s expert, Dr. Liao, admitted that he has never, 

himself, written a scientific paper about a strain with multiple genes knocked out and reported fewer 

321(...continued) 

finds that Ajinomoto failed to disclose the best mode of practicing claim 15 of the ‘ 160 patent as of 

the December 8 1993 date of the Japanese priority application, “the only result would be that 

Ajinomoto could not rely on the 1993 Japanese application filing date, but instead would have to 

reply on the 1994 PCT application filing date.” CIB at 2 1. Both GBT and the Staff argues that 

Ajinomoto has waived this argument. The undersigned agrees. Ground Rule 8.2 explicitly states 

that: 

the pretrial brief shall set forth with particularity a party’s contentions on each of the 

proposed issues . . . Any contentions not set forth in detail as required herein shall 

be deemed abandoned or withdrawn, except for contentions of which a party is not 

aware and could not be aware in the exercise of reasonable diligence at the time of 

filing the pre-trial brief. 

Since Ajinomoto could have, but did not, set forth this contention in its pre-hearing brief, the 

undersigned finds that Ajinomotoj has waived this argument. Notably, Ajinomoto never argues that 

December 8, 1993 is not the effective filing date of claim 15 of the ‘ 160 patent. RFF 1.71 (“Thus, 

the effective filing date of claim 15 is December 8, 1993.”) (no dispute). 

322 RIB at 28. 

323 Id. 

324 Id. 

325 Id. at 28-29. 

63 
than all of the knocked out genes.326 GBT also relies on the testimony of its own expert, Dr. Webb, 

who disagreed with Kojima’s argument that W3llO(tyrA) is really just an abbreviation for 

W3 1 lO(tyrA, ty~-R).~~~ 

With regard to strain B-399, GBT asserts that according to the patent, strain B-399 was 

derived from strain B-3996 by removing the pVIC40 plasmid from B-3996.328 GBT argues that the 

results reported in the ‘160 patent for strain B-399 must be fictitious because data obtained with 

another strain derived from an AEC-resistant strain of [ 1 and 

inserting certain other genes designed to optimize lysine biosynthesis showed lower results than those 

disclosed in the patent.329 Specifically, GBT asserts that the [ 3 derivative described above with 

the additional genes designed to optimize lysine production produced [ 3 lysine, while disclosed 

strain B-399 without the additional genes allegedly produced 9.2 g/L lysine.330 Given these results, 

GBT argues that “there is every reason to believe that if the inventors had actually used B-399, that 

strain would not have produced the results recited in the patent.”331 

Like GBT, the Staff also argues that a fictitious example in the ‘ 160 patent constitutes a best 

mode violation.332 Specifically, the Staff argues that the specification of the ‘ 160 patent provides 

fictitious information relating to strain W3 1 lO(tyrA) because Ajinomoto’s research records do not 

contain any experiment wherein such a strain was used prior to the filing of the Japanese priority 

326 Id. at 29. 

327 Id. 

328 Id. 

329 Id. 

330 Id. 

33’ Id. 

332 SIB at 36. 

64 
application in December 1993.333 According to the Staff, Kojima admits that he did not actually use 

a W3 1 1 O(tyrA) strain.334 

Ajinomoto asserts that GBT’s argument that there is fictitious data in the 160 patent amounts 

to little more than “if Ajinomoto did not retain the underlying data, then it must be fabricated.”335 

According to Ajinomoto, many of Ajinomoto’s records, which were written fifteen years ago, no 

longer Specifically, Ajinomoto asserts that Japan has a first to file patent system and that 

under that system documents underlying an invention served no purpose to establish priority and thus 

at the time of the effective filing date of the ‘698 patent, Ajinomoto did not require its inventors to 

keep their laboratory notebooks and allowed them to maintain them or dispose of them as they saw 

fit.337 Ajinomoto asserts that it was not until 1996 that Ajinomoto changed its retention policy.338 

With regard to the ‘ 160 patent specifically, Ajinomoto argues that Kawamura and Ogawa performed 

the purportedly fictitious experiments, but that their lab notebooks were not kept.339 Ajinomoto also 

argues that both Kojima and Liao testified that the allegedly fictitious strain W3310(tyrA) was the 

same as the W31 lO(tyrR tyrA) strain disclosed in the patent.340 According to Ajinomoto, Kojima 

dropped the “tyrR” designation from the patent because that particular mutation was irrelevant, a fact 

on which Ajinomoto asserts its expert Liao agrees.341 Additionally, Ajinomoto argues that it was 

acceptable in scientific publications to abbreviate strain designations to delete mutations that are not 

333 Id. 

334 Id. 

335 CIB at 37. 

336 Id. 

337 Id. 

338 Id. 

339 Id. at 38. 

340 Id. 

341 Id. 

65 
relevant to the publication.342 

Under the heading “BEST MODE FOR CARRYING OUT THE INVENTION,” the ‘160 

patent states that “[t] he present invention will be more concretely explained below with reference to 

Examples.”343 Examples 1-5 of the patent describe how to mutate dapA on a plasmid and transform 

a host strain with the resulting mutant plasmid for an Escherichia organism.344 Specifically, the ‘ 160 

patent discloses introducing the mutant dapA gene into an Escherichia organism using host strains 

B-399 and W3 1 The patent discloses the results of three experiments using strains B-399 

and W3 1 1 O(tyrA) that purport to illustrate the invention of claim 1 5 .346 Table 7 purports to illustrate 

the production of lysine using strain W3 1 1 O(tyrA) transformed with plasmid RSFDSO, which harbors 

both mutant dapA and mutant lysC genes.347 The data reported in Table 7 indicates that strain 

W3 1 1 O(tyrA) transformed with the RSFD80 plasmid produced 8.9 g/L lysine, while the control 

produced 0 g/L lysine.348 

Although the results disclosed in Table 7 purport to be the results from an experiment using 

strain W3 1 1 O(tyrA)/RSFDSO, the evidence of record indicates that no such strain was ever used by 

the inventors of the ‘ 160 patent. In fact, inventor Kojima admits that the actual strain used was strain 

W3 1 1 O(tyrR ~Y~A)/RSFDSO.~~~ Because strain W3 1 lO(tyrR tyrA) was actually used and not strain 

342 Id. 

343 JX-1 at 17:63-67. 

344 Id. at 18:l-30:30. 

345 Id. 

346 Id. at Tables 5-7. 

347 Id. at 29:34-30:30. 

348 Id. at Table 7. 

349 See CX-235C (Kojima WS) at 7 270 (“The tyrR gene is the regulatory gene for the 

biosynthetic genes of phenylalanine and tyrosine. TyrA gene codes prephenate dehydrogenase. . . . W3 1 10 (tyrR tyrA) was used as a host strain for testing the mutations for lysine biosynthesis.”). 

66 
W3 1 1 O(tyrA) as disclosed in the ‘ 160 patent, the results shown in Table 7 are fictitious. 

Ajinomoto asserts that W3 1 lO(tyrR tyrA) is the same as W3 1 lO(tyrA), arguing that 

W3 1 1 O(tyrA) is simply an abbreviation for strain W3 1 1 O(tyrR tyrA).”’ However, even Ajinomoto’s 

expert Liao admits the two strains are different stating that “one is a two knockout, one is a one 

knockout, of course, they are different.”351 This is consistent with the testimony of GBT’s expert 

Webb who stated that: 

the designations of genotype in strains is a very precise science and tyrA, tyrR 

deficiencies, or a combination thereof within a bacterial strain means very different 

things, and so to in fact say that it’s just an abbreviation for something else that was 

meant, I find, from a scientific standpoint, that to be very difficult to understand why 

he would say that.”352 

Further, while Kikuchi alleges that WC196 is really shorthand for WC80-196S, none of the 

meticulously kept monthly reports or research reports from the Lysine Project refers to W3 1 10(tyrR 

tyrA) as W3 1 1 O(tyrA). 

Accordingly, for the reasons discussed above, the undersigned finds that the evidence of 

record clearly and convincingly shows that Table 7, and the data presented therein, are fictitious. The 

Federal Circuit has held that the disclosure of fictitious data in support of a best mode disclosure in 

a patent is a violation of the best mode requirement of Section 1 12.353 Thus, undersigned finds claim 

15 ofthe ‘160 patent invalid under 35 U.S.C. $1 12. 

350 See CX-235C (Kojima WS) at 7 271; see also CORFF 2.22. 

351 Liao, Tr. 1345:16-1346:4. 

352 Webb, Tr. at 1070:16-1071:lO. 

353 See, e.g. Hoffmann-La Roche, Inc. v. Promega Corp., 323 F.3d 1354, 1367 (Fed. Cir. 

2003); Consolidated Aluminum Corp. v. Fonseca Int’l Ltd., 910 F.2d 804, 808 (Fed. Cir. 1990); 

Certain Salinomycin Biomass and Preparations Containing Same, Inv. No. 337-TA-370, Pub. No. 

2978, ID at 46-47 (July 1996), afd sub nom. Kaken Pharm. Co. v. Int ’I Trade Comm ’n., 1 1 1 F.3d 

143 (Fed. Cir. 1997) (“Salinomycin”). 

67 
3. Obviousness 

GBT argues that claim 15 of the ' 160 patent would have been obvious to one of ordinary skill 

in the art as of the filing date of the Japanese priority patent application, December 8, 1993.354 

According to GBT, the parties agree that all but one of the elements of claim 15 were well known in 

the art.355 GBT asserts that every aspect of claim 15 was well known as of the filing date of the 

Japanese priority patent application except for the specific mutations to dapA, which GBT argues are 

Specifically, GBT argues that the only element as to which there is any serious debate is the 

following element of claim 3, on which claim 15 depends: 

a DNA coding for a DDPS originating from a bacterium belonging to the genus 

Escherichia and having mutation to desensitize feedback inhibition by L-lysine, 

wherein the mutation is selected from the group . . .357 

On this point, GBT argues that the enzyme encoded by dapA (DDPS) had long been understood to 

be one of two significant choke-points in lysine biosynthesis because of the fact that it was feedbackinhibited.358 Thus, GBT argues one seeking to enhance lysine biosynthesis in E.coli would be 

motivated to mutate dapA to desensitize it.359 According to GBT, the dapA gene had been isolated 

and sequenced in 1986, thus making it readily accessible.360 Additionally, GBT asserts that AEC, a 

chemical analog of lysine, was well known to be useful for selecting feedback desensitized mutants.361 

354 RIB at 30. 

355 Id. 

356 Id. 

357 Id. at 31. 

358 Id. at 32. 

359 Id. 

360 Id. 

36' Id. at 33. 

68 
GBT asserts that in 1972, Herman et al. used AEC to select feedback-desensitized dapA mutants of 

the genus Pseudomonas. GBT argues that the work of Herman et al. was transferable to E.coli 

because the two organisms have similar metabolic and physiological functions and have identical 

lysine biosynthetic pathways.362 GBT also asserts that in 1992, Bittel et al. transformed E.coli cells 

lacking the dapA gene with maize dapA, mutagenized them, and selected AEC-resistant mutants.363 

According to GBT, these mutants had feedback-desensitized maize DDPS.364 GBT asserts that its 

expert, Dr. Somerville, testified that the work done by Bittel and his colleagues was “conceptually 

identical” to the work done by the inventors of claim 15 of the ‘ 160 patent.365 GBT further asserts 

that Ajinomoto’s expert, Dr. Liao, conceded that it would be reasonable to try the approach 

demonstrated by Bittel et al.366 Additionally, GBT asserts that both Somerville and Webb have 

testified that a researcher performing in vitro mutagenesis on the dapA gene followed by AEC 

selection would obtain at least one of the two identified mutations.367 According to GBT, the 

Ajinomoto researchers did not specifically target the specific amino acid residues at the 8 lst and 1 1 Sth 

positions, but instead simply followed known selection techniques and sequenced the resulting 

mutants.368 

Like GBT, the Staff also argues that claim 15 of the ‘ 160 patent would have been obvious to 

one of ordinary skill in the art as of the December 8,1993, filing date of the Japanese priority patent 

362 Id. 

363 Id. 

364 Id. 

365 Id. 

366 Id. 

367 Id. at 34. 

368 Id. 

69 
application.369 In particular, the Staff argues that the inventors of the '160 patent merely applied 

known and widely-used techniques to a known gene, dapA, to minimize andor block its production 

of a known enzyme (DDPS) in the biosynthetic pathway for production of lysine in order to obtain 

the mutated bacteria covered by claim 3 of the ' 160 patent.370 The Staff asserts that as of 1986, the 

wild-type E.coli dapA gene had been isolated and sequenced.371 The Staff also asserts that there were 

many known methods of obtaining mutant E.coli bacteria with desensitized dapNlysC genes to 

increase production of lysine and that such mutated E.coli bacteria had been used to produce 

lysine.372 Thus, the Staff argues the only difference between the alleged invention of claim 15 of the 

' 160 patent and the prior art is that the inventors of the ' 160 patent isolated the mutated dapA gene 

and sequenced it to determine the specific location of the mutation(^).^^^ 

More specifically, the Staff argues that one following customary mutagenesis/AEC selection 

procedures would create a bacteria that inevitably would have a mutation at one or more of the 

specific sites set forth in claim 3 because only a small number of sites exist where lysine could bind 

on the DDPS enzyme.374 The Staff argues that the physical interaction between lysine and DDPS 

causes a change in the shape of that enzyme, that the shape of the enzyme helps the enzyme to carry 

out its biological hction, that any alteration of the shape can alter the activity of the enzyme, and 

that given the small size of lysine compared to the enzyme one would expect that there would be only 

369 SIB at 40. 

370 Id. 

371 Id. at 41. 

372 Id. 

373 Id. 

374 Id. at 42. 

70 
a small number of actual sites of binding on the DDPS enzyme.375 Thus, the Staff argues that, while 

many mutations may have occurred within the gene, the limitation imposed by the selection process 

on the products of mutagenesis limits the results to a very small number.376 Of this small number of 

surviving mutants, the Staff argues that there is a very high probability that the survivors would have 

mutations at the 8 1 st and 1 18th 

Ajinomoto asserts that GBT admits that none of the prior art references it relies on discloses 

the specific mutations recited in claim 15 of the ' 160 patent.378 Ajinomoto argues that GBT and the 

Staff make no attempt to show that the prior art suggests the claimed mutations.379 Instead, according 

to Ajinomoto, GBT and the Staff present only a generalized discussion regarding desensitization of 

the dapA gene.380 Ajinomoto argues that GBT and the Staff, without any reference to the prior art, 

simply recite GBT's experts' conclusions that had a person of ordinary skill in the art performed AEC 

selection and mutagenisis, that person would have discovered at least one of the two mutations recited 

in claim 3.381 Ajinomoto argues that this is nothing more than after-the-fact hindsight analysis.382 

Ajinomoto asserts that there is no evidence that the prior art could be used as GBT suggests to obtain 

the specific mutations recited in claim 15 of the ' 160 patent.383 Ajinomoto argues that the lysine 

binding site on DDPS of E.coli was not known in 1993 and, without that knowledge, there was no 

method to predict accurately the specific amino acid changes that would promote feedback 

375 Id. 

376 Id. 

377 Id. at 42-43. 

378 CRE3 at 26. 

379 Id. at 27. 

380 Id. 

381 Id. 

382 Id. 

383 Id. 

71 
inhibition.384 Ajinomoto argues that the obviousness case against claim 15 of the ‘ 160 patent boils 

down to GBT arguing that if one of ordinary skill in the art did what no one except the Ajinomoto 

inventors thought to do, that person would have reached the same result as in claim 1 5.385 

The determination of obviousness is a question of law based on underlying factual inquiries 

into the (1) the scope and content of the prior art, (2) the level of ordinary skill in the art, (3) the 

differences between the claimed invention and the prior art ; and (4) secondary considerations of nonobviousness (also known as “objective evidence”). The undersigned has determined, supra, that a 

person of ordinary skill in the art to which the ‘ 160 patent pertains would have an advanced degree 

in Biology, Biochemistry, Genetics, Genomics, Microbiology, Molecular Biology, Agricultural 

Engineering, or Metabolic Engineering with 3-5 years of experience in a laboratory specializing in 

genetic engineering. The undersigned also found, supra, that persons with a Bachelor’s degree could 

also be skilled in the art, but only after on-the-job training under the direct supervision of a Ph.D.- 

level scientist. See supra, at 1V.D. 1. 

As of December 1 993, the filing date of the Japanese priority patent application, the evidence 

of record shows that fermentation was already being used to produce lysine and thus, one of ordinary 

skill in the art at the time would know that fermentation could be used for the production and 

accumulation of lysine.386 The record also shows that the cultivation of lysine produced by 

fermentation was also known. Additionally, the evidence shows that in 1982, Dauce-Le Reverend 

384 Id. 

385 Id. 

386 See RX-88C (Somerville WS) at 7 33; see aZso CX-23 1C (Liao WS) at 7 46-47; JX-1 at 

1 : 12-1 3. 

72 
et al. disclosed a lysine producing E.coli strain.387 Also in 1982, US Patent No. 4,346,170 ("the ' 170 

patent") issued, which disclosed lysine production inE.~oli.~" In fact, the ' 160 patent itself notes that 

AEC resistant strains of the genus Escherichia were known in the prior art to be lysine producers.389 

Even Ajinomoto's expert, Liao, testified that he had "seen some prior art articles . . . about the use 

of E.coli to produce lysine.390 Thus, one of ordinary skill in the art at the time would know generally 

that E.coli could be used to produce lysine. The evidence also shows that as of December 1993, the 

steps along the lysine biosynthesis pathway in Escherichia were 

The prior art also includes a 1962 Yugari and Gilvarg reference that establishes that the lysine 

biosynthesis pathway involves enzymes that are feedback-inhibited by lysine.392 In 1976, a prior art 

reference by Patte, et al. disclosed more particularly, two enzymes in the pathway that were subject 

to feedback inhibition by lysine: DDPS (dapA gene) and AKIII (lysC gene).393 In 1986, the evidence 

of record shows that Richaud et al. isolated and sequenced the dapA gene.394 

Prior to the work of Patte, et al. and Richaud, et al., in 1972 Hermann, et al. published a study 

in which AEC was used to select feedback-desensitized dapA mutants of the genus Pseudomonas.395 

Also in the prior art is a 1992 reference by Bittel, et al. The evidence of record shows that Bittel, et 

al. successfully transformed E.coli cells lacking the dapA gene with maize dapA, mutagenized them, 

387 

388 

3 89 

390 

391 

300-305. 

392 

393 

394 

395 

See JX-123; RX-89C (Webb WS) at 7 335. 

See RX-163; RX-89C (Webb WS) at 7 334. 

JX-1 at 1:15-19; RX-89C (Webb WS) at 77 295-96; JX-117. 

Liao Tr. at 1423:6-9. 

See Liao, Tr. 1426:14-17; RX-88C (Somerville WS) at 7 25; RX-89C (Webb WS) at 71 

JX-179; RX-89C (Webb WS) at 7 301. 

JX-156; RX-89C (Webb WS) at 7 302. 

See JX-161; Liao, Tr. 1426:23-25; RX-89C (Webb WS) at 77 303. 

See JX-120; Liao, Tr. 1450:19-1451:7; RX-88C (Somerville WS) at 77 33,36. 

73 
and selected AEC-resistant mutants.396 Specifically, Bittel, et al. used AEC selection techniques to 

isolate the DDPS gene from maize, inserted it into a plasmid, transformed a strain of E.coli that 

lacked the dapA gene, subjected the bacteria to mutagenesis and selected AEC-resistant strains.397 

According to the record evidence, the selected AEC-resistant strains had feedback desensitized maize 

DDPS.398 

In addition to that which is cited above, the record evidence shows that as of the December 

1993 filing date of the Japanese priority patent application, the following techniques were known and 

available to researchers for performing tasks within molecular biology: PCR, the use of 

endonucleases and ligases to create plasmids, mutagenesis through agents like NTG or 

hydroxylamine, gene sequencing, use of multiple copy plasmids to increase gene expression, in vitro 

mutagenesis of a target gene on a plasmid, and AEC selection to identifl feedback desensitized 

mutants.399 

What is not disclosed in the prior art, but what is claimed in claim 15 of the' 160 patent is an 

Escherichia bacteria that has a mutant dapA gene of E.coli at the 8 1 st or 1 18th amino acid residue of 

the DDPS enzyme causing desensitization to feedback inhibition by lysine.400 While GBT and the 

Staff argue that creating such a bacteria would have been obvious to one of ordinary skill in the art 

at the time of the filing of the Japanese priority patent in December 1993, the evidence of record does 

not support such a conclusion, especially not clearly and convincingly. Moreover, GBT and the Staff 

396 See JX-119; Liao, Tr. 1444:16-14455-8; RX-88C (Somerville WS) at 77 44. 

397 RX-88C (Somerville WS) at 17 44. 

398 See JX-119; RX-88C (Somerville WS) at 71 46. 

399 See Liao Tr. at 1424:l-1425:22; see also RX-89C (Webb WS) at 77 306, 307, 309-12, 

400 CX-231C (Liao WS) at 7 192; see also RIB at 30. 

331-33,337,339. 

74 
incorrectly frame the obviousness inquiry. The invention of claim 15 is not merely directed to an 

Escherichia strain with the specific mutations recited in claim 3 of the ‘160 patent, but rather a 

method of producing, accumulating and cultivating ly~ine.~” Thus, the proper obviousness inquiry 

is whether one of ordinary skill in the art as of December 8, 1993 would have found it obvious to 

produce lysine using a bacteria from the genus Escherichia that has a mutant E.coli dapA gene at the 

8 1 st or 1 18th amino acid residue of the DDPS enzyme. 

Having properly defined the scope of the inquiry it becomes plain that GBT and the Staff 

impermissibly used hindsight in concluding that claim 15 was obvious. Notably, GBT’s expert 

Somerville admitted at the hearing that the steps he testified one of ordinary skill in the art could 

follow to get to the invention, are the very same steps taken by the inventors and described in the ‘ 160 

patent.402 GBT and the Staffs case for obviousness amounts to little more than an argument that 

because the tools and techniques necessary to create an Escherichia strain with the specified E.coli 

mutant dapA gene were available and known to one of ordinary skill in the art in December 1993, 

claim 15 must be obvious. The Supreme Court, however, recently reaffirmed the impropriety of such 

an approach, stating that “a patent composed of several elements is not proved obvious merely by 

demonstrating that each of its elements was, independently, known in the prior art.”403 In so 

reaffirming, the Supreme Court acknowledged the continued importance of identifying “a reason that 

would have prompted a person of ordinary skill in the relevant art to combine the elements in the way 

401 See 35 U.S.C. 3 103 (A claim is obvious if “the differences between the subject matter 

sought to be patented and the prior art are such that the subject matter as a whole would have been 

obvious at the time the invention was made to a person having ordinary skill in the art to which said 

subject matter pertains.”)(emphasis added). 

402 Somerville, Tr. at 1285:15-1286:12, 1251:lO-14. 

403 KSR, 127 S.Ct. 1727, 1741 (2007). 

75 
the claimed new invention Additionally, the Federal Circuit in interpreting KSR has noted 

that “the Supreme Court suggests, a flexible approach to the TSM test prevents hindsight and focuses 

on evidence before the time of in~ention.’’~~~ Further, the Federal Circuit has more recently stated that 

“[tlhe TSM test, flexibly applied, merely assures that the obviousness test proceeds on the basis of 

evidence-teachings, suggestions (a tellingly broad term), or motivations (an equally broad term)-that 

arise before the time of invention as the statute requires.”406 

GBT argues that it would have been an obvious choice in December 1993 to use Escherichia 

(or at least E.coli) as the host strain for lysine production. However, the evidence shows that there 

were inherent difficulties in using E.coli for lysine fermentation, not the least of which being that 

E.co1i is not a natural lysine Moreover, at the time, Corynebacterium was being used 

almost exclusively for the production of lysine.408 Thus, while Ajinomoto may have had a specific 

motivation as a result of the competitive threat from Archer Daniels Midland (“ADM’) to begin 

looking for nonconventional ways to more efficiently produce lysine, there is no evidence that anyone 

else would have been so motivated.409 

404 See Takeda Chem. Indus. Ltd. v. Alphapharm Pty, Ltd., 492 F.3d 1350,1356-57 (Fed. Cir. 

405 In re Translogic Tech., Inc., 504 F.3d 1249, 1257 (Fed.Cir. 2007). 

406 Ortho-McNeil Pharmaceutical, Inc. v. Mylan Laboratories, Inc., 520 F.3d 1358, 1365 

407 See CX-234C (Kikuchi WS) at 76; CX-235C (Kojima WS) at T[ 23. 

408 CX-231C (Liao WS) at T[ 46,44,48; see also Somerville, Tr. at 1235:9-13. 

409 See CX-235C (Kojima WS) at 7 7 (stating that the origin of theLysine Project began “[iln 

1990, [when] Ajinomoto concluded that it was at a competitive disadvantage to Archer Daniels 

Midland (“AD,”) in the production of L-lysine. ADM has access to its own internal glucose 

supplies at a much lower cost than Ajinomoto. Companies like ADM, who have separate sugar 

processing operations, generate huge quantities of glucose that can be used as the raw material to 

make amino acids through fermentation.”), f 78 (“In order to compete with Archer Daniels Midland, 

we attempted to improve the quality of the bacterial strain that is used in a fermentation process to 

(continued. ..) 

2007)(quoting KSR). 

(Fed.&. 2008). 

76 
As is typical when impermissibly relying on hindsight to conclude obviousness, GBT and the 

Staff fail to provide any reason why one of ordinary skill in the art at the time would have combined 

or modified the many prior art referekes cited to get to the claimed invention of claim 1 5 of the ' 160 

patent. Notably, several prior art references relied on by GBT and the Staff were disclosed and 

considered by the PTO during the prosecution of the ' 160 patent. Thus, GBT's burden of showing 

invalidity is especially difficult!" 

With regard to the 1962 Yugari and Gilvarg reference and the 1976 Patte reference, GBT 

contends that the fact that the references disclose that the lysine biosynthesis pathway involves 

feedback-inhibited enzymes that one seeking to enhance lysine biosynthesis would be motivated to 

mutate the dapA gene to desensitize it.411 However, the evidence of record does not support such a 

finding. Mainly, the references fail to disclose whether or how alterations to the feedback-inhibited 

enzymes would affect the function of the lysine biosynthesis pathway.412 Additionally, the record 

evidence indicates that merely knowing that an enzyme is subject to feedback inhibition is insufficient 

to determine whether that enzyme plays an important role in E.coli's lysine biosynthesis pathway.413 

With regard to the 1986 Richaud reference, one of the references cited by the PTO in the ' 160 

patent, GBT contends that the fact the reference disclosed the sequence for the E.coli dapA gene 

meant that dapA could be isolated and mutated.414 However, the evidence of record does not support 

409(. . .continued) 

produce lysine. We hoped that we could overcome the cost advantage that Archer Daniels Midland 

had in the raw materials with an improvement in the bacteria used in the fermentation process."). 

410 See Hewlett-Packard Co. v. Bausch & Lomb, Inc., 909 F.2d 1464,1467 (Fed. Cir. 1990). 

411 RIB at 32. 

412 See JX-179. 

413 See CX-235C (Kojima WS) at fly 29-30. 

414 RIB at 32. 

77 
a finding that by simply knowing the sequence for the E.coli dapA gene that one of ordinary skill in 

the art in December 1993 would be able to discover the specific mutations claimed in the ' 160 patent 

or identify the mutations by their specific lysine binding 

With regard to the 1972 Hermann et al. reference, another reference cited by the PTO in the 

' 160 patent, GBT contends that because this reference discloses the use of AEC to select feedbackdesensitized dapA mutants of the genus Pseudomonas that one of ordinary skill in the art in December 

1993 would know that AEC could be used to select feedback-desensitized dapA mutants in the genus 

E~chericia.~'~ At the hearing, GBT's expert Somerville went so far as to testify that the 1972 

Hermann et al. reference rendered claim 15 of the '160 patent obvious as of the date of the 

reference.417 Notably, however, Somerville was unable to come up with any explanation why if the 

claimed invention was obvious in 1972 that no one else came up with the embodiment of claim 15 

before Ajinomoto did in 1993, some 21 years later. Contrary to GBT's contention with regard to 

Hermann et al., the evidence of record contains nothing that would lead one to believe that the 

teachings derived from Pseudomanas strains would be transferable to strains of a completely different 

genus, Escherichia.418 In addition, the evidence fails to show that any researcher extended the work 

of Hermann et al. to E.~oli.~'~ 

With regard to the 1992 Bittel et al. reference, another reference cited by the PTO in the ' 160 

patent, GBT contends that the fact that the reference discloses transforming E.coli cells lacking the 

415 CX-231C (Liao WS) at 7 190. 

416 RIB at 33. 

417 Somerville, Tr. at 1252:17-1253:20. 

418 See CX-231C (Liao WS) at 7 197; see also CX-167 at 5 (1975 Halsall reference 

disclosing that use of AEC selection with E.coli failed to identify mutatnt dapA gene encoding 

desensitized DDPS.). 

419 Id. 

78 
dapA gene with maize dapA, mutagenizing them, and selecting AEC-resistant mutants, that one of 

ordinary skill in the art at the time of the filing of the Japanese priority patent application in December 

1993 would have been motivated to apply the same techniques to E.coli in an effort to achieve E.coli 

with desensitized dapA gene.42o However, the evidence of record suggests that the lysine insensitive 

form of maize DDPS disclosed by Bittel et al. is more sensitive to lysine than wild-type E.coli 

DDPS.421 Sommerville provides no evidence that using the methodology disclosed in Bittel et al. 

would have identified mutant genes that are much less sensitive to lysine than the mutant maize 

genes. Additionally, while Bittel et al. discloses mutagenized transformed E.coli cells, the ' 160 patent 

discloses mutant dapA genes obtained via in vitro mutagenesis.422 

As discussed above, GBT and the Staff use impermissible hindsight to sift through the prior 

art to conclude that claim 15 of the ' 160 patent is obvious. While Webb and Somerville's pathway 

to the invention may in retrospect seem to follow logical steps using available tools and techniques 

to come to the invention of claim 15, at the time of the invention the inventor's insights and 

willingness to confront and overcome obstacles cannot be discounted. Accordingly, for the reasons 

discussed above, the undersigned finds that GBT and the Staff failed to prove by clear and convincing 

evidence that claim 15 of the ' 160 patent was obvious as of the date of the filing of the Japanese 

priority patent application on December 8, 1993. 

4. Obviousness Double-Patenting 

GBT argues that claim 15 of the '160 patent is invalid under an obviousness-type double 

patenting analysis because it is not patentably distinct from claim 1 of commonly owned U.S. Patent 

420 RIB at 33. 

421 See CX-231C (Liao WS) at 7 195; Liao, Tr. at 1444:16-1445:14. 

422 See JX-119; JX-1. 

79 
No. 4,278,765 (“the ‘765 patent”).423 GBT argues that claim 1 of the ‘765 patent discloses a method 

for obtaining bacteria of any genus that can produce amino acids. According to GBT, claim 1 recites 

transforming a recipient host bacterium with a plasmid carrying genes controlling the synthesis of the 

desired amno acid (i. e., genes along the biosynthesis pathway of the desired amino GBT also 

asserts that claim 1 requires that the inserted genes be mutated to destroy the negative regulation of 

the synthesis (i. e., the mutation must destroy feedback inhibition) of the desired amino a~id.4~~ GBT 

notes that claim 1 of the ‘765 patent is not limited to any particular amino GBT argues that 

the only elements of claim 15 of the ‘ 160 patent that do not appear in claim 1 of the ‘765 patent would 

have been obvious to one skilled in the Specifically, GBT argues that it would have been 

obvious to transform a host with “genes controlling the synthesis of a selected amino acid,” viz., with 

dapA mutated to destroy “the negative regulation” (i.e., feedback inhibition), and sequence the 

resulting mutants.428 GBT asserts that it “is very likely that some of the resulting mutants would have 

been identical to those GBT further argues that it would have been obvious to cultivate 

the bacterium in a culture medium to accumulate and collect lysine.430 

The Staff argues that claim 15 of the ‘160 patent is invalid for obviousness-type double 

patenting in light of the commonly owned ‘765 patent.431 The Staff sets forth two arguments in 

423 RIB at 37. 

424 Id. 

425 Id. 

426 Id. 

427 Id. at 39. 

428 Id. 

429 Id. 

430 Id. 

431 SIB at 44. 

80 
support.432 First, the Staff argues that claim 15 of the ‘ 160 is not patentably distinct from claim 1 of 

the ‘765 patent because claim 1 of the ‘765 patent anticipates claim 3 of the ‘160 patent, and the 

limitations added by claim 15 are obvious.433 The Staff does not elaborate on this argument in its 

brief, but rather incorporates by reference its argument in its pre-hearing brief.434 Ground Rule 1 1.1 

states that “the post-hearing brief shall discuss the issues and evidence tried within the framework of 

the general issues determined by the Commission’s Notice of Investigation, the general outline of the 

briefs as set forth in Appendix B, and those issues that are included in the pre-trial brief and any 

permitted amendments thereto. All other issues shall be deemed Additionally, 

incorporating arguments by reference unfairly circumvents the page limits imposed on the parties in 

this investigation. Because the Staff did not develop this argument in its post-hearing brief, the 

undersigned finds the argument waived. Second, the Staff argues that to the extent claim 1 of the 

‘765 patent does not anticipate claim 3 of the ‘ 160 patent, that claim 3 is obvious for the reasons set 

forth in its post-hearing brief regarding obvousness under 35 U.S.C. 9 103.436 

Ajinomoto argues that GBT’s expert Webb finds double patenting “by piecing apart each 

element of claim 15 of the ‘ 160 patent and then plugging in the elements of the ‘765 patent as he sees 

fit.”437 Ajinomoto asserts that as compared to claim 15 of the ‘ 160 patent, claim 1 of the ‘765 patent 

does not disclose: (1) limitations directed to producing, accumulating and collecting lysine in a 

culture; (2) the dapA gene itself; (3) the DDPS enzyme; or (4) the specific mutations recited in claim 

432 Id. 

433 Id. 

434 Id. (“See Staff prehearing brief at 43-47.”). 

435 Ground Rule 1 1.1 (emphasis added). 

436 Id. 

437 CIB at 60. 

81 
15 of the ‘160 patent.438 According to Ajinomoto, GBT’s expert Webb admits that the above 

limitations are missing from claim 1 of the ‘756 patent.439 Ajinomoto argues that based on the above 

differences it cannot be said that the two claims a “SO very much alike.”440 Ajinomoto argues that 

claim 1 of the ‘765 patent may be broad enough to cover practice of claim 15 of the ‘ 160 patent, but 

the fact that a claim in an earlier patent dominates a claim in a later patent does not, mean that the 

later claim is invalid for double patenting.441 

Non-statutory or “obviousness-type” double-patenting is a judicially created doctrine adopted 

to prevent claims in separate applications or patents that do not recite the “same” invention, but 

nonetheless claim inventions so alike that granting both exclusive rights would effectively extend the 

life of the patent Generally, an obviousness-type double patenting analysis entails two 

steps. First, as a matter of law, the claim in the earlier patent is construed and the claim in the later 

patent is construed and the differences between the two are determined. Second, the court determines 

whether the differences in the subject matter between the two claims renders the claims patentably 

distinct. A later claim that is not patentably distinct from an earlier claim in a commonly owned 

patent is invalid for obviousness-type double patenting.443 A later patent claim is not patentably 

distinct from an earlier patent claim if the later claim is obvious over, or anticipated by, the earlier 

438 Id. 

439 Id. 

440 Id. 

441 Id. 

442 Georgia-Pacflc Corp. v. US Gypsum Co., 195 F.3d 1322, 1326 (Fed. Cir. 1999). 

443 In re Metroprolol Succinate Patent Litigation, 494 F.3d 101 1, 1016 (Fed. Cir. 2007); 

444 Eli Lilly and Co. v. Barr Laboratories, Inc., 25 1 F.3d 955,968 (Fed. Cir. 2001). 

Perricone v. Medics Pharmaceutical Corp., 432 F.3d 1368, 1371-73 (Fed. Cir. 2005). 

82 
Claim 1 of the ‘765 patent is a claim directed to “[a] method for preparing bacterial strains.”445 

Claim 15 of the ‘ 160 patent is directed to “[a] method for producing lysine.”446 As Ajinomoto points 

out and GBT’s expert Webb admits, claim 1 of the ‘765 patent differs from claim 15 of the ‘ 160 

patent in that claim 1 of the ‘765 patent fails to disclose: (1) limitations directed to producing, 

accumulating and collecting lysine in a culture; (2) the dapA gene; (3) the DDPS enzyme; or (4) the 

specific mutations recited in claim 15 of the ‘ 160 patent.447 Relying on the same evidence it presents 

in support of its contention that claim 15 of the‘160 patent is obvious under 35 U.S.C. tj 103, GBT 

argues that these missing limitations would have been obvious in light of the prior art references and 

tools and techniques known to one of ordinary skill in the art as of December 1993. 

However, for the same reasons discussed in detail, supra, with regard to GBT’s Section 103 

obviousness contention, the undersigned finds that claim 1 5 of the ‘ 160 patent is patentably distinct 

from claim 1 of the ‘765 patent and thus not invalid for obviousness-type double patenting. While 

claim 1 of the ‘765 patent may be broad enough to cover practice of claim 15 of the ‘ 160 patent, the 

fact that a claim in an earlier patent dominates a claim in a later patent does not mean that the later 

claim is obvious. In particular, the undersigned finds that GBT and the Staff fail to provide any 

reason why one of ordinary skill in the art as of December 1993, with claim 1 of the ‘765 patent in 

hand, would choose to cultivate lysine using a bacteria from the genus Eschericia with the specific 

mutations claimed in claim 15 of the ‘ 160 patent. Again, GBT and the Staff fail to give proper credit 

to the inventor’s insights and willingness to confront and overcome obstacles in achieving the 

invention embodied in claim 1 5. 

445 See Rx-164 at 12:2. 

446 See JX-1 at 68:l-5. 

447 Compare JX-1 with RX-164; see also Webb, Tr. at 1004: 17-25, 1006: 1-20. 

83 
E. Unenforceability - Inequitable Conduct 

GBT and the Staff argue that the ‘160 patent is unenforceable because the best mode 

information Ajinomoto concealed was inherently material, and the omission was deliberate and 

intentional, thus evidencing an intent to deceive the PT0.448 GBT also argues that a pattern of 

nondisclosure, concealment and fictitious examples also supports an inference of intent.449 

Specifically, GBT and the Staff argue that Ajinomoto’s failure to disclose their best mode of 

practicing claim 15 of the ‘ 160 patent (i. e., the AE-70 strain) and their best mode of practicing claim 

22 of the ‘ 160 patent (i.e., the TA-325 strain) are both material, because best mode is a requirement 

of patentability. 450 Likewise, GBT and the Staff argue that Ajinomoto’s disclosure of fictitious 

examples regarding both claim 15 and claim 22 of the ’ 160 patent is also material for the same 

reasoning. With regard to intent, GBT argues that “it is difficult to imagine an acceptable reason for 

disclosing fictionalized data.”’””’ GBT and the Staff also argue that the Ajinomoto inventors 

deliberately withheld their best mode With regard to claim 15 in particular, GBT argues 

that Kawamura testified that according to Kojima, the reason she was named an inventor on the patent 

was because she developed a highly productive lysine-producing strain (i. e., AE-70), and yet the 

strain for which she was named an inventor was not GBT and Staff additionally argue 

with regard to both claim 15 and claim 22, that internal, confidential research reports show that the 

inventors linked AE-70 to the Japanese priority patent application and TA-325 to the PCT application, 

448 RIB at 41; SIB at 49. 

449 RIB at41. 

450 SIB at 50, 54. 

451 RIB at 42. 

452 SIB at 50, 51, 54. 

453 RIB at 42. 

84 
thus evincing that the inventors were aware that the patents were closely related to their work on AE70 and TA-325, but chose not to disclose them.454 GBT further argues o:the subject of intent that 

the fact that Ajinomoto failed to disclose their best mode strains for both claims 15 and 22 and instead 

disclosed fictitious examples for both claims shows a pattern of nondisclosure and misrepresentation 

that strongly suggests that the conduct was no accident. 

Ajinomoto argues that GBT and the Staffs inequitable conduct argument fails both the 

materiality and intent prongs.455 With regard to materiality, Ajinomoto argues that since there was 

no best mode violation with respect to claim 15 and claim 22 GBT cannot establish materiality.456 

With regard to intent, Ajinomoto asserts that the inventors testified that they did not intend to deceive 

anyone with respect to either AE-70 or TA-325.457 Ajinomoto argues that the undersigned was in a 

position to judge the credibility of the ‘160 inventors and see that GBT’s argument is baseless.458 

Ajinomoto also asserts that Japan has no best mode requirement, arguing that GBT cannot explain 

how one can have an intent to deceive where there is no opportunity for deception.459 Additionally, 

Ajinomoto asserts that claim 22 did not exist in the 1994 PCT application, arguing that GBT has not 

presented any evidence that the inventors could have intended in 1994 to break a rule that applies to 

a claim that had not yet been drafted.460 Further, with regard to GBT’s argument that the confidential 

research reports show that the inventors linked AE-70 to the Japanese priority patent application, 

Ajinomoto argues: (1) that there is no reference in JX-45C to AE-70 as being the “best,” but rather 

454 Id.; SIB at 51. 

455 CIB at 41. 

456 Id. 

457 Id. at 43. 

458 Id. 

459 Id. 

460 Id. 

85 
the reference is to AE-70 having the "highest yield" sometime during the period covered by the 

research report; (2) that the sentence following that reference recognized that the lysine production 

ability of the strain is [ 3 and (3) the reference to the patent application was written in August 

or September 1994, after the December 1993 patent application and long after AE-70 was abandoned, 

so the author of the research report could not have been validating AE-70."61 

As discussed above, GBT and the Staff argue that the ' 160 patent is unenforceable because 

the patent applicants intentionally failed to disclose their best mode for claims 15 and 22 and because 

the applicants included fictitious examples in the patent specification. The undersigned has already 

determined, supra, that the inventors violated the best mode requirement of Section 1 12 with regard 

to claim 15 for failing to disclose their preferred host strain AE-70 as of the Japanese priority date of 

December 8,1993. The undersigned has also found, supra, that the inventors violated the best mode 

requirement by including fictitious examples in support of their best mode of practicing claim 15 of 

the ' 160 patent. However, the undersigned has not yet adjudicated GBT and the Staffs allegation that 

the inventors' violated the best mode requirement by failing to disclose their preferred host strain for 

practicing claim 22 of the ' 160 patent. Accordingly, before GBT and the Staffs inequitable conduct 

argument can be addressed, GBT and the Staffs best mode argument with regard to claim 22 must 

be considered. 

a. Best mode of claim 22 

Claim 22 depends from claim 16. Claim 22 reads as follows: 

22. A method of producing L-lysine, comprising: 

cultivating the bacterium of claim 16 in a suitable culture medium, 

46' Id. at 44. 

86 
producing and accumulating L-lysine in the culture thereof, and 

collecting L-lysine from the culture.“62 

Independent claim 16 reads as follows: 

16. A bacterium belonging the genus Escherichia which is transformed 

with a DNA coding for a dihydrodipicolinate synthase originating 

from a bacterium belonging to the genus Escherichia and having 

mutation to desensitize feedback inhibition by L-lysine, and 

further harboring an aspartokinase which is desensitized to feedback 

inhibition by L-lysine, and wherein a dihydrodipicolinate reductase 

gene is enhanced.463 

Claim 16 is directed to an Escherichia bacterium that is transformed with: (1) Escherichia DNA 

coding for DDPS that has been mutated to desensitize feedback inhibition by lysine; (2) a mutant of 

the gene encoding for aspartokinase; and (3) a mutant of the gene encoding for dihydrodipicolinate 

reductase.464 The gene encoding for aspartokinase is known as The gene encoding for 

dihydrodipicolinate reductase is known as dapB.466 The effective filing date for claim 22, and claim 

16 on which it depends, is the date of the filing of the PCT application on November 28, 1 994.467 

Looking first to the claims of the ‘160 patent, the undersigned finds that the preamble 

language of claim 22 clearly and unambiguously sets forth the utility of the claimed invention, namely 

“producing L-ly~ine.”~~~ As set forth in claim 22, the production of L-lysine includes at least the 

following three steps: (1) cultivating the bacterium of claim 16 in a suitable culture medium (ie., A 

462 JX-1 at 68:37-41. 

463 Id. at 68:6-14. 

464 RFF 1.61 (no dispute). 

465 RFF 1.62 (no dispute). 

466 RFF 1.63 (no dispute). 

467 RFF 1.73 (no dispute). 

468 See Northern Telecom, 2 15 F.3d at 1287 n. 1 (“Preamble language in a claim may provide 

an indication of how the inventor intended to ‘carry out’ his invention.”). 

87 
bacterium belonging to the genus Escherichia having mutations to the dapA gene, dapB gene, and 

lysC gene.); (2) producing and accumulating L-lysine in the culture thereof; and (3) collecting Llysine from the culture.469 Thus, according to the plain language of claim 22, the claimed invention 

includes the overall production of L-lysine, as well as, the cultivation of an Escherichia bacterium 

with the specific mutations to the dapA, dapB and lysC genes and the accumulation and collection 

of the L-lysine. The specification confirms that the invention of the ‘ 160 patent is not simply directed 

to the mutations to the dapA, dapB, and lysC genes, but to a bacterium belonging to the genus 

Escherichia having the mutation to the dapA, dapB, and lysC genes and an improved method for 

producing L-lysine using said Thus, based on the plain language of the claims, as 

supported by the specification, the undersigned finds the claimed invention of claim 22 of the ‘ 160 

patent to encompass the overall production of L-lysine, including the cultivation of an Escherichia 

bacterium with the specific mutations to the dapA, dapB, and lysC genes, and the accumulation and 

collection of the L-lysine. 

Turning to the first prong in the best mode analysis, the undersigned finds for the reasons 

discussed below that as of the time of the filing of the PCT application on November 28, 1994, the 

inventors had a subjective preference for using host strain TA-325 to practice claim 16 of the ‘ 160 

patent. Specifically, the monthly reports and research reports generated during the Lysine Project 

clearly and convincingly show the inventors preference for strain TA-325. For example, in Research 

469 See JX-1 at 68:6-14,37-41. 

470 See id. at 4:30-37; see also id. at 1:l-2 (“METHOD OF PRODUCING L-LYSINE BY 

FERMENTATION”), 4:66-5:4 (“The present invention fhther provides a method of producing Llysine comprising the steps of cultivating any of the bacterium belonging to the genus Escherichia 

described above in an appropriate medium, producing and accumulating L-lysine in a culture thereof, 

and collecting L-lysine from the culture.”). 

88 
Report No. 7, covering the period between September 1993 and May 1994, Ogawa reported that TA325 with the pCABD2 plasmid (which included mutant dapA and lysC and enhanced dapB) was the 

“maximum yield lysine-producing ba~teria.’~~’ Additionally, in Research Report No. 9, covering the 

period from April 1993 through March 1994, Kojima and Kawamura reported that by using the TA325 strain “in March 1994 we finally achieved our target of [ Kojima and 

Kawamura also reiterated that “[tlhe TA-325 strain had the highest production ability.”473 Moreover, 

in Research Report No. 13, which covered the period from April 1994 through September 1994, 

Ogawa wrote that TA-325 was “the best” lysine-producing bacteria.474 Further, in the monthly report 

for October 1994, just one month before the PCT application was filed, Kawamura referred to TA325 as “the current Additionally, the monthly reports and research reports show that the 

inventors were achieving results using the TA-325 strain that exceeded the results reported for the 

disclosed strains in the ‘ 160 patent.476 

] with [ 

As previously discussed, Ajinomoto argues that the TA-325 strain was not the inventors’ 

preferred host strain because the TA-325 strain still had unresolved problems as of the filing date of 

the PCT application. However, the fact that the TA-325 strain had not been perfected prior to the 

filing of the PCT application is irrelevant to the determination of whether the inventors had a 

subjective preference for strain TA-325 at the time ofthe PCT filing. The fact that the TA-325 strain 

may have had objective problems cannot thwart the clear and convincing evidence that the inventors 

471 JX-52CT at AHL003 105. 

472 JX-96CT at AHL436044. 

473 Id. at AHL436056. 

474 JX-53CT at AHL003 163. 

475 JX-46CT at AHL430675. 

476 See e.g., JX-28CT at AHL430720; JX-31CT at AHL430712; JX-98CT at AHL436092; 

JX-58CT at AHL436376. 

89 
had a subjective preference for strain TA-325 as of November 28,1994. The undersigned finds the 

evidence on which Ajinomoto relies does not overcome the clear and convincing documentary 

evidence discussed in detail, supra, that shows that the inventors had a subjective preference for TA325. Accordingly, for the reasons set forth hereinabove, the undersigned finds based on the 

documentary evidence of record that the inventors of the ' 160 patent had a subjective preference for 

the TA-325 host strain at the time of filing the PCT application on November 28, 1994. 

Having determined that the inventors had a subjective preference for the TA-325 host strain 

at the time of filing the PCT application, the best mode analysis turns to the second prong to 

determine whether the inventors' disclosure is adequate to enable one of ordinary skill in the art to 

practice the best mode of the invention. As previously discussed, this second prong is objective and 

depends on the scope of the claimed invention and the level of skill in the relevant art. Because the 

scope of the claimed invention encompasses the host strain and the evidence shows that the inventors 

had a subjective preference for the TA-325 host strain at the time of filing the PCT application, the 

inventors were obligated under Section 1 12 to disclose that preference. There can be no question that 

the TA-325 strain was not disclosed in the ' 160 patent.477 Thus, the undersigned finds the ' 160 patent 

disclosure insufficient to enable one of ordinary skill in the art to practice the inventors' preferred 

embodiment of the invention as claimed in claim 22 of the ' 160 patent, viz., the TA-325 host strain 

transformed with dapA, dapB, and lysC mutants. 

For the reasons discussed herein, the undersigned finds that Ajinomoto's concealment of its 

preferred embodiment of claim 22 of the ' 160 patent to be a violation of the best mode requirement 

of 35 U.S.C. 5 112. 

477 See JX-1. 

90 
b. Inequitable conduct 

The undersigned has found, supra, several violations of the best mode requirement with 

respect to the ‘ 160 patent. Specifically, the undersigned has found that the inventors failed to disclose 

their preferred best mode for practicing claims 15 and 22 of the ‘160 patent. Additionally, the 

undersigned has held that the inventors’ inclusion of fictitious data in the specification to support the 

patentability of claim 15 is also a best mode violation. 

There can be no doubt based on the evidence of record that the inventors of the ‘160 patent 

knew of the preferred AE-70 strain at the time of the filing of the Japanese priority application in 

December 1993 and of the TA-325 strain at the time of the filing of the PCT application in November 

1994. The Federal Circuit has held that “[blecause disclosure ofthe best mode is statutorily required, 

see 35 U.S.C. 0 1 12, failure to disclose the best mode is inherently material and, we believe, reaches 

the minimum level of materiality necessary for a finding of inequitable Accordingly, the 

undersigned finds the above described best mode violations are material. 

With regard to intent, the record evidence shows that Ajinomoto engaged in a pattern of nondisclosure in procuring the ‘ 160 patent, including the inventors’ failure to disclose their preferred host 

strain for practicing claim 15 in December 1993 when they filed their Japanese priority application, 

and their failure to disclose their preferred host strain for practicing claim 22 in November 1994, 

when they filed their expanded PCT application. Notably, Ajinomoto’s repeated failure to disclose 

its best lysine producing host strains comes during a time when the record evidence indicates 

Ajinomoto was facing increased business competition from ADM. Moreover, the record evidence 

See ConsolidatedAluminum, 9 10 F.2d at 808 (citing J. P. Stevens & Co., Inc. v. Lex Tex 

Ltd., Inc., 747 F.2d 1553, 1559 (Fed. Cir. 1984)). 

91 
shows that Ajinomoto also made a series of misrepresentations in procuring the ‘ 160 patent, including 

the explicit description in the specification that describes how to create what has been determined to 

be a fictitious host strain, W3 1 lO(tyrA), and the inclusion of fictitious data in Table 7 to support the 

patentability of claim 15. Ajinomoto’s intentional inclusion of fictitious information and data, 

coupled with its repeated failure to disclose the inventors’ true best mode for practicing claims 15 and 

22 of the ‘160 patent, leads the undersigned to the inescapable conclusion that Ajinomoto had an 

intent to deceive when it filed its patent application. Because both the materiality and intent elements 

are high, equity demands a finding of inequitable conduct. Accordingly, based upon strong evidence 

of specific acts of concealment and misrepresentation by the applicants in connection with the ‘ 160 

patent, the undersigned finds by clear and convincing evidence that the ‘ 160 patent is unenforceable 

due to inequitable conduct before the PT0.479 

V. The ‘698 Patent 

A. Claim Construction 

1. Asserted Claims 

Claim 15 is the only asserted claim of the ‘698 patent. Claim 15 of the ‘698 patent depends 

from claim 13, which in turn depends from independent claim 3. Claim 15 reads as follows: 

15. 

Escherichia coli. 

The method of claim 13, wherein the microorganism belongs to the species 

Claim 13 reads as follows: 

13. A method for producing L-lysine, comprising: 

(a) cultivating the microorganism of claim 3 in a liquid medium, 

479 Kingsdown, 863 F.2d 867 (Fed. Cir. 1988); Sulinomycin, Inv. No. 337-TA-370, 

Unreviewed Initial Determination, 1995 WL 1049822 (U.S.I.T.C. November 6, 1995). 

92 
thereby producing the L-lysine and accumulating the L-lysine in the 

liquid medium, and 

(b) collecting the L-lysine produced and accumulated in step (a). 

Independent claim 3 reads as follows: 

3. An isolated microorganism belonging to the genus Escherichia, 

wherein the microorganism contains a mutant of a wild-type gene 

encoding a wild-type lysine decarboxylase; 

the microorganism lacks the wild-type gene encoding the wild-type 

lysine decarboxylase; 

the wild-type lysine decarboxylase comprises the amino acid sequence 

of SEQ ID NO:4; and 

the mutant gene encodes no lysine decarboxylase having 

decarboxylating activity, the mutant gene encodes a mutant lysine 

decarboxylase having less decarboxylating activity than the wild-type 

lysine decarboxylase, or the mutant gene contains a mutation in a 

regulatory region causing the microorganism to produce less of the 

wild-type lysine decarboxylase than a microorganism containing the 

wild-type gene encoding the wild-type lysine decarboxylase. 

2. Disputed Claim Limitations 

There are no disputed claim limitationsper se. However, GBT and the Staff argue that the 

‘698 patent at issue is invalid for failing to satisfy the best mode requirement of 35 U.S.C. $ 112. As 

previously stated, the contours of the best mode analysis are defined by the scope of the claimed 

invention, which in turn is determined by applying the ordinary principles of claim construction. 

Thus, in this regard, the parties do dispute how the scope of the claimed invention is construed. 

However, this dispute is more appropriately resolved, infia, when analyzing GBT and the Staffs best 

mode argument. 

93 
B. Infringement 

Ajinomoto and GBT stipulate that GBT’s manufacture ofL-lysine feed products using the Old 

Escherichia bacterium strain deposited with the ATCC under Accession #SD-5590 infiinges claim 

15 of the ‘698 patent.480 Ajinomoto and GBT also stipulate that GBT’s manufacture of L-lysine 

products using the Corynebacterium strain deposited with the ATCC under Accession #SD-5620 does 

not infringe Claim 15 of the ‘698 patent.481 Additionally, Ajinomoto and GBT stipulate that GBT’s 

manufacture of L-lysine products using the New Escherichia bacterium strain deposited with the 

ATCC under Accession #SD-57 17 does not infringe Claim 15 of the ‘698 patent.482 Based on the 

stipulation, the undersigned finds that: (1) GBT’s manufacture of L-lysine feed products using the 

Old Escherichia bacterium strain deposited with the ATCC under Accession #SD-5590 infringes 

claim 15 of the ‘698 patent; (2) GBT’s manufacture of L-lysine products using the Corynebacterium 

strain deposited with the ATCC under Accession #SD-5620 does not infringe Claim 15 of the ‘698 

patent; and (3) GBT’s manufacture of L-lysine products using the New Escherichia bacterium strain 

deposited with the ATCC under Accession #SD-5717 does not infringe Claim 15 of the ‘698 patent. 

C. 

Ajinomoto and GBT stipulate that Heartland uses the method of Claim 15 of the ‘698 patent 

to make L-lysine Based on the stipulation, the 

undersigned finds that Ajinomoto practices claim 15 ofthe ‘698 patent. Accordingly, the undersigned 

finds that Ajinomoto satisfies the technical prong ofthe domestic industry requirement of Section 337 

Domestic Industry - Technical Prong 

The Staff does not dispute this 

480 JX-190C at 7 10. 

481 Id. atl11. 

482 Id. at 7 12. 

483 Id. at 7 5. 

484 See CFF 3.22 (no dispute). 

94 
with regard to the asserted ‘698 patent. 

D. Validity 

1. Ordinary Skill in the Art 

The parties propose the same definitions of one of ordinary skill in the art that they proposed 

for’the ‘ 160 patent, supra. Accordingly, for the same reasons discussed with regard to the ‘ 160 

patent, the undersigned finds a person of ordinary skill in the art to which the ‘698 patent pertains 

would have an advanced degree in Biology, Biochemistry, Genetics, Genomics, Microbiology, 

Molecular Biology, Agricultural Engineering, Metabolic Engineering with 3-5 years of experience 

in a laboratory specializing in genetic engineering. The undersigned also finds that persons with a 

Bachelor’s degree could be skilled in the art, but only after on-the-job training under the direct 

supervision of a Ph.D.-level scientist. 

2. Best Mode 

The first task in the best mode analysis is to define the invention claimed in the ‘698 patent. 

In defining the invention, the parties make virtually identical arguments to the ones they made with 

regard to the ‘ 160 patent. Ajinomoto argues that the inventors of the ‘698 patent fully disclosed the 

invention and the best mode of carrying it out by disclosing the best mode of making the specific 

mutation to the ldc gene.485 As with the ‘ 160 patent, Ajinomoto argues that the scope of the claimed 

invention of the ‘698 patent is limited to the claimed mutation, viz., the mutant ldc gene. GBT and 

the Staff argue, however, that the scope of the claimed invention is not limited to the mutation to the 

ldc gene. Rather, GBT and the Staff argue that the scope of the claimed invention encompasses the 

production of lysine using a bacteria of the species E.coli with mutant ldc gene, the accumulation of 

485 CIB at 9. 

95 
the lysine and its collection. As with the ‘160 patent, GBT and Staff argue that Ajinomoto’s 

interpretation of the claimed invention impermissibly reads out explicit claim limitations of claim 15 

of the ‘698 patent. 

Looking first to the claims of the ‘698 patent, the undersigned finds that the preamble 

language of claim 13, on which asserted claim 15 depends, clearly and unambiguously sets forth the 

utility of the claimed invention, namely “producing L-ly~ine.”~’~ As set forth in claim 13, the 

production of L-lysine includes at least the following steps: (1) cultivating the microorganism of 

claim 3 (i.e., a microorganism belonging to the species k.coli having a mutant ldc gene) in a liquid 

culture medium; (2) producing and accumulating L-lysine in the liquid medium; and (3) collecting 

the produced and accumulated L-ly~ine.~’~ Thus, according to the plain language of claim 13, the 

claimed invention includes the overall production of L-lysine, as well as, the cultivation of an E.coli 

microorganism with the mutant ldc gene, and the accumulation and collection of the L-lysine. 

Having examined the claims, the specification is consulted. The specification confirms that 

the invention of the ‘698 patent is not simply directed to the mutation to the ldc gene, but to a 

microorganism belonging to the species E.coli having the mutation to the ldc gene and an improved 

method for producing L-lysine using said microorganism. For example, the specification states that 

“an object of the present invention is to obtain a novel lysine decarboxylase gene of Escherichia coli, 

create an L-lysine producing microorganism belonging to the genus Escherichia with restrained 

expression of the gene and/or the cadA gene, and provide a method or producing L-lysine by 

486 See JX-2 at 32:34; Northern Telecom, 215 F.3d at 1287 n.1 (“Preamble language in a 

487 See JX-2 at 3 1 : 19-36, 32:34-40. 

claim may provide an indication of how the inventor intended to ‘carry out’ his invention.”). 

96 
cultivating the rnicroorgani~m.”~~~ The Federal Circuit has recognized that the use of the phrase 

“present invention” puts the public on notice as to the scope of the invention as a whole.489 

Thus, based on the plain language of the claims, as supported by the specification, the 

undersigned finds the claimed invention of claim 15 of the ‘698 patent to encompass the overall 

production of L-lysine, including the cultivation of an Escherichia coli microorganism with a 

mutation to the ldc gene, and the accumulation and collection of the L-lysine. The undersigned 

rejects Ajinomoto’s argument that the scope of the claimed invention should be limited to the 

mutation to the ldc gene for the reasons discussed, supra, with regard to the ’ 160 patent, including 

that Ajinomoto’s argument impermissibly reads explicit limitations out of claim 15 ofthe’698 patent. 

Having defined the invention of claim 15 of the ‘698 patent, the undersigned turns to GBT’s 

specific arguments supporting its contention that there has been a violation of the best mode 

requirement with regard to claim 15 of the ‘698 patent. GBT makes three separate arguments: (1) that 

the Ajinomoto inventors failed to disclose their preferred host strain; (2) that the Ajinomoto inventors 

failed to disclose their preference for sucrose as a carbon source; and (3) that the disclosed best mode 

was Each argument will be addressed in turn below. 

488 See JX-2 at 1 :46:52; see also id. at 1 : 1-2 (“LYSINE DECARBOXYLASE GENE AND 

METHOD OF PRODUCING L-LYSINE”), 2:7-10 (“[Tlhe present invention provides a 

microorganism belonging to the genus Escherichia . . .”), 2: 1 1-1 7 (“[Tlhe present invention provides 

a method of producing L-lysine comprising the steps of cultivating, in a liquid medium, a 

microorganism belonging to the genus Escherichia described above to allow L-lysine to be produced 

and accumulated in a culture liquid, and collecting it.”). 

489 See, e.g., Honeywell Int ’I Inc. v. ITT Indus., Inc., 452 F.3d 13 12, 13 18 (Fed. Cir. 2006); 

Alloc, Inc. v. US. Int ‘I Trade Comm’n, 342 F.3d 1361, 1378 (Fed. Cir. 2003). 

490 RIB at 48-55. 

97 
a. The Ajinomoto inventors failed to disclose their preferred host 

strain 

GBT argues that as of the time of filing the ‘698 patent, on December 9,1994, the inventors 

had only one host strain for practicing claim1 5, a strain denominated WC80-196S.49’ GBT asserts 

that Ajinomoto failed to disclose the WC80-196s host strain in the ‘698 patent. GBT argues that 

Ajinomoto’s failure to disclose the only mode they actually contemplated for carrying out the 

invention is a violation ofthe best mode requirement of 35 U.S.C. 5 1 12.“92 GBT asserts that to create 

WC80-196S, the inventors took two additional steps that are not disclosed in the specification of the 

‘698 patent. Specifically, GBT argues that the inventors replaced the lysC gene on the chromosome 

with a feedback desensitized lysC mutant before exposing the cells to NTG mutation and the 

inventors inserted a package of five sucrose-utilization genes into the chromosome of the host 

GBT asserts that Kikuchi admitted at trial that a skilled artisan would not realize from the patent’s 

best mode description that the host strain was created by replacing the lysC gene before 

metagenesis.494 GBT also asserts that Kikuchi agreed that the ‘698 patent does not disclose the 

introduction of the sucrose utilization genes.495 Additionally, GBT argues that Ajinomoto should be 

estopped from arguing that one of ordinary skill would have known to add sucrose utilization genes, 

because Ajinomoto recently obtained U.S. Patent No. 7,179,623 (“the ‘623 patent”) which covers the 

sucrose utilization genese Ajinomoto failed to disclose in the ‘698 ~atent.4~~ 

Ajinomoto argues that GBT has failed to adduce clear and convincing evidence of a best mode 

491 Id. at 48. 

492 Id. 

493 Id. 

494 Id. at 51. 

495 Id. 

496 Id. at 49. 

98 
violation.497 Ajinomoto asserts that the ‘698 patent is directed to the reduction or elimination of 

lysine decarboxylation by modification of the ldc gene, arguing that there can be no best mode 

violation because the inventors made the novel ldc gene available by public deposit.498 Ajinomoto 

also argues that the inventors disclosed the nucleotide sequence of the ldc gene.499 With regard to 

GBT’s allegation that the inventors failed to disclose their use of a modified lysC gene prior to NTG 

mutagenesis, Ajinomoto asserts that Dr. Kikuchi did not know if the use of a modified lsyC gene prior 

to NTG mutagenesis worked and that according to Dr. Liao’s testimony it probably did not.s00 Thus, 

Ajinomoto argues there is no scientific basis for calling the use of a modified lysC gene prior to 

mutagenesis a “best mode.”501 According to Ajinomoto, a belief that an experiment may yield 

positive results is not a “best mode” where there is no evidence that an experiment actually 

succeeded.s02 Additionally, Ajinomoto argues that the only point of introducing the lysC mutant was 

to try to enhance lysine biosynthesis, which was a property of mutant lysC genes already known in 

the art at the time of filing.s03 Ajinomoto asserts that it is undisputed that the ‘698 patent discloses 

using a desensitized lysC gene. Further, Ajinomoto argues that Kikuchi publically deposited strain 

WC80-196, which was created using a modified lysC gene prior to NTG mutagene~is.’~~ 

With regard to GBT’s allegation that the inventors failed to disclose the use of sucrose 

utilization genes, Ajinomoto argues that Kikuchi believed that the choice of sugar had nothing to do 

497 CIB at 30. 

498 Id. 

499 Id. 

Id. at 31. 

501 Id. 

. Id. at 35. 

503 Id. at 33. 

504 Id. at 31. 

99 
with the claimed invention.505 According to Ajinomoto, the evidence shows that glucose is better than 

sucrose and is still the preferred carbon source because it is usually cheaper than sucrose.5o6 

Ajinomoto argues that it used glucose almost exclusively and that its own experiments never 

established that sucrose was a better carbon source.5o7 Ajinomoto also argues that at the time of filing, 

one skilled in the art would know that sucrose could be used as a carbon source for E.coli simply by 

adding sucrose utilization genes and that one skilled in the art would know how to insert the 

utilization genes.508 Additionally, Ajinomoto asserts that there were at least a dozen articles published 

on the subject at the time of the effective filing date of the ‘698 patent.509 Further Ajinomoto asserts 

that GBT’s expert, Dr. Webb, agreed that one or ordinary skill would have known to add sucrose 

utilization genes to use sucrose as a carbon source and how to do it.510 

As previously discussed, the first part of the best mode inquiry is subjective and asks whether 

the inventors had a preferred embodiment in mind at the time the patent application was filed. 

Inventor Kikuchi testified at the hearing that before the filing of the ‘698 patent, strain WC80-196s 

and its derivatives were the only strains from which he had knocked out the ldc gene.511 According 

to Kikuchi’s hearing testimony, Research Report No. 10 and the strain development chart of Exhibit 

RX-64C disclose the method used to create the WC80-196s strain.512 At his deposition, however, 

505 Id. at 32. 

506 Id. 

507 Id. at 33. 

508 Id. at 31. 

509 Id. 

510 Id. at 32. 

511 See Kikuchi, Tr. at 702:17-21 (“Q. And before the filing of the patent, the strain 

WC80-196s and its derivatives were the only strains from which you had knocked out the ldc gene, 

right? A. That is correct.”). 

512 See id. at 625:20-626:1,626:25-627:22; RFF 3.62 (no dispute); see also JX-51CT; RX- 

(continued ...) 

100 
Kikuchi more candidly admitted that Research Report No. 10 and the strain development chart 

showed the “best way” known to him at the time for creating the host.strain WC80-196S.513 

Specifically, Research Report No. 10, covering the period from December 1993 through March 1994, 

describes the methodology used to create strain WC80-196s as follows: 

(1) When RSFDSO is introduced into E.coli strain W3 1 10-derived Phe-producing 

bacterial host that produces Lys as the sole byproduct amino acid and Lys-producing 

cultivation is performed, it shows a high [ ] yield, suggesting high latent 

capabilities for strain W3 1 10 Lys production, and furthermore, effectiveness in giving 

nutritional demands. 

(2) To obtain AEC-resistant strains from strain W3 1 10, we obtained strain WC80 

with lysC on chromosomes substituted with desensitized-type lysC80 through 

homologous substitution. 

(3) We obtained approximately 800 AEC-resistant strains by processing strain 

WC80 with NG, and selected nine high Lys-producing strains (1 -2g/L) through testtube cultivation. 

(4) We gave sucrose utilization capability by transducing strain B399 sucroseutilizing genes to the aforementioned nine strains using PI phages. Furthermore, when 

we introduced plasmid pCABl which has lysC80, dapA*24 and dapB to these strains 

and performed Lys-producing cultivation using sucrose as C-source, strain WC80- 

196S/pCABl showed a [ ] yield.514 

Stated more succinctly, to create strain WCSO-196s the inventors: (1) replaced the chromosomal copy 

ofthe lysC gene of E.coli W3 1 10 with a feedback-desensitized mutant, thereby creating strain WC80; 

(2) subjected the lysC-replaced cells to NTG mutagenesis; (3) selected colonies able to survive in 

512(...continued) 

64C. 

513 Kikuchi, Tr. 700:5-12 (“QUESTION: So looking at the research report, Exhibit 51, and 

the summary of the steps in it, which is Exhibit 64, those are the sources that show the best way 

known to you at the time of creating a host strain that you could then use for disruption or deletion 

of the lysine decarboxylase genes, right? ANSWER: I believe so.”). Kikuchi, Tr. 700:5-12 

(“QUESTION: So looking at the research report, Exhibit 5 1, and the summary of the steps in it, 

which is Exhibit 64, those are the sources that show the best way known to you at the time of 

creating a host strain that you could then use for disruption or deletion of the lysine decarboxjrlase 

genes, right? ANSWER: I believe so.”). 

514 JX-5 1 CT at AHL003 185. 

101 
AEC; (4) chose a colony having L-lysine productivity, thereby creating strain WC80-196; and (5) 

inserted sucrose utilization genes into strain WC80-196, thereby creating host strain WC80-1 96S.5’5 

Inventor Kikuchi documented his reasons for following the above steps in Research Report No. 1 0.5’6 

For example, with respect to the first step of replacing the lysC gene of strain W3 1 10 with a feedbackdesensitized mutant, Kikuchi explained that: 

The initial plan was to obtain AEC-resistant strains by mutating wild E.coli strain 

W3 1 10. However, when AEC-resistant strains are introduced in E.coli wild strains, 

it is reported that bacterial strains are obtained for which lysC has been desensitized 

for most of the strains. Desensitized-type has already been obtained for lysC, which 

is also easy to amplify with plasmids. Therefore, in order to obtain bacterial strains 

that have mutation points in various places other than lysC, we thought to substitute 

the lysC on chromosomes with desensitized type lysCS0 bef~rehand.~’~ 

Ajinomoto’s argument that Dr. Kikuchi did not know if the use of a modified lsyC gene prior 

to NTG mutagenesis worked and thus there was no scientific basis for calling the use of a modified 

lysC gene prior to mutagenesis a “best mode” is misplaced. The first step in the best mode inquiry 

is focused on the inventors subjective belief at the time of filing and not whether that belief has an 

objective basis for support. Thus, the fact that Kikuchi did not know if using a modified lysC gene 

prior to NTG mutation produced positive results is immaterial as the evidence shows that Kikuchi 

had a clear preference for using strain WC80-196s to practice claim 15 of the ‘698 patent. Moreover, 

Kikuchi’s testimony at the hearing is belied by Kikuchi’s written comments in Research Report No. 

10, which shows that Kikuchi thought that lysC replacement prior to mutagenesis was important in 

developing a lysine-producing host strain.518 In fact, at the hearing, Kikuchi testified that with regard 

515 See CX-234CT (Kikuchi WS) at 77 40-42,45,54; see also RX-64C. 

516 See JX-5 1 CT. 

517 Id. at AHL003 180. 

518 See JX-51CT at AHL003176; Kikuchi, Tr. 785:16-786:3, 821:21-822:7. 

102 
to lysine production, the lysC replacement was the “number one key step.”519 

Ajinomoto argues more generally that Kikuchi did not have a best strain in mind at the time 

of the December 9, 1994, effective filing date of the ‘698 patent. However, the evidence of record 

shows that strain WC80-196s was the only strain the Ajinomoto inventors used to practice claim 15 

of the ‘698 patent.520 Because the WC80-196s strain was the only strain that the inventors used, it 

must necessarily be the best strain they had at the time of the effective filing date of the patent. 

Moreover, the evidence shows that Kukuchi clearly preferred to create the host strain by first 

incorporating a mutated lysC gene into the chromosome before subjecting the organism to 

mutagenesis, followed by AEC selection, and incorporating sucrose utilization genes into the cells 

that survived the selection process that produced high lysine yields.521 In light of the documentary 

evidence and testimony, the undersigned finds Ajinomoto’s argument that Kikuchi did not have a best 

mode in mind at the time of the filing of the ‘698 patent unpersuasive. 

Accordingly, the undersigned finds for the reasons discussed above that as of December 9, 

1994, the Ajinomoto inventors had a subjective preference for the WC80-196s strain as the 

microorganism used to practice claim 15 of the ‘698 patent. 

Having determined that the inventors had a subjective preference for the WC80-196s strain, 

the next step in the best mode analysis if to determine whether the specification of the ‘698 patent 

would have enabled one of ordinary skill in the art at the time of the invention to practice 

Ajinomoto’s best mode, or in other words, whether the inventors concealed their best mode fiom the 

519 Kikuchi, Tr. 647:20-648:2. 

520 Id. at 702: 17-2 1. 

521 See, e.g., JX-5 1 CT at AHL003 185. 

103 
publi~.~” The purported best mode for practicing claim 15 of the ‘698 patent is described in the 

patent under the heading “Best Mode For Carrying Out The Invention.”523 Under the subheading 

“Preparation of Escherichia coli having L-lysine productivity,” the patent purports to describe the best 

way of preparing the host strain that is used to practice claim 15.524 The patent describes the 

following three steps for producing a host strain: (1) subject cells of E.coli W3 1 10 to N-methy1-N’- 

nitro-N-nitrosoguanidine mutation treatment; (2) select colonies able to survive in the lysine analog 

AEC; and (3) choose a colony having L-lysine productivity.525 According to the patent, a host strain 

obtained using these steps is denominated WC196.526 Also according to the patent specification, a 

host strain allegedly produced according to these steps was deposited by the Aj inomoto inventors 

under accession number FERM P- 1 4690.527 Notably, however, the deposited strain was not WC 196 

as the specification states, but rather a strain denominated WC80-1 96.528 

The method described in the specification for creating the host strain used to practice claim 

15 of the ‘698 patent fails to explicitly recite two steps taken by the inventors in creating their 

preferred host strain, WC80-196s. Specifically, the patent fails to describe the steps of inserting a 

mutant lysC gene prior to mutagenesis and AEC selection, and adding sucrose utilization genes. 

Because the description in the patent is written as if those were the steps actually performed in 

creating the host strain, the fact that two additional steps taken by the inventors were not disclosed 

leads to the conclusion that the patent specification is a misrepresentation of what was actually done 

522 See Chemcast, 913 F.2d at 928. 

523 JX-2 at 7:18-19. 

524 Id. at 8:40-41. 

525 Id. at 8:40-63. 

526 Id. at 855-63. ’’’ Id. 

528 Kikuchi, Tr. at 718-19; see also RFF 3.43 (no dispute). 

104 
by the inventors. 

Although the patent specification fails to disclose two of the steps taken by the inventors in 

creating their preferred host strain WC80- 196S, Ajinomoto argues that the specification nevertheless 

satisfies the objective prong of the best mode requirement because the specification of the ‘698 patent 

discloses the use of a desensitized lysC gene and persons of ordinary skill in the art knew of prior art 

disclosures that taught incorporation of a desensitized lysC gene before mutagenesis and the 

incorporation of sucrose utilization genes into E.coli was well known in the art. As discussed in more 

detail below, the undersigned finds Ajinomoto’s arguments without merit. 

The specification describes the incorporation of a desensitized lysC gene as one of five 

potential methods that could be used to increase production of lysine by the micr~organism.~~~ Thus, 

the specification does not inform one of ordinary skill which method, ifany, was used by the 

inventors in creating their preferred host strain. Further, Kikuchi admitted that the disclosure of the 

‘698 patent would not place one of ordinary skill in the art on notice that the insertion of the lysC 

mutation had been done prior to NTG mutation.530 

With regard to the sucrose utilization genes, whether one of ordinary skill in the art would 

have known how to insert sucrose utilization genes into a strain is of no moment, because there is no 

disclosure in the ‘698 patent that would suggest to one of ordinary skill in the art that such was the 

inventors’ preference or that it was beneficial to do so. The fact is, the starting strain disclosed in the 

‘698 patent, W3 1 10, was known by those of skill in the art not to be able to naturally use sucrose.531 

Further, the evidence shows that Ajinomoto did not just incorporate any sucrose utilization genes in 

529 JX-2 at 5:20-67. 

530 See Kikuchi, Tr. at 823-24. 

531 Kikuchi, Tr. at 650, Liao, Tr. at 1406. 

105 
their preferred WC80-196s host strain, but rather incorporated the specific utilization genes that 

Ajinomoto obtained the ‘623 patent on some thirteen years later.532 The ‘623 patent includes claim 

1, which states: 

A method for producing an amino acid selected from the group consisting of 

isoleucine, lysine, and valine comprising: 

a) cultivating in a culture medium which contains sucrose as a carbon source 

a bacterium belonging to the genus Escherichia which has been constructed from a 

sucrose non-assimilative strain belonging to the genus Escherichia , wherein said 

bacterium harbors sucrose PTS genes from Escherichia coli VKPM B-7915 and has 

an ability to produce said amino acid, and 

b) collecting said amino acid from said medium.533 

During prosecution of the ‘623 patent, in response to an anticipation rejection from the PTO, 

Ajinomoto argued that its invention was patentable because the reference cited by the examiner did 

not teach the production of lysine and did not teach that the “production of. . . lysine . . . was higher 

when the bacterium of the present invention is cultivated in a medium which contains sucrose, as 

opposed to glucose, as the carbon source.”534 If the use of sucrose PTS genes in an E.coli bacteria to 

produce lysine was patentable in 2007, it is hard to even begin to understand how Ajinomoto could 

argue that as of the effective filing date of the ‘698 patent in 1994 one or ordinary skill in the art 

would have known to incorporate such genes in a host strain to practice claim 15 of the ‘698 patent. 

Ajinomoto also argues that the omissions in the ‘698 patent are of no matter because the 

inventors deposited their preferred strain. However, it is undisputed that the deposited strain, 

deposited under accession number FERM P- 14690, fails to include the sucrose utilization genes found 

532 See RFF 3.154 (no dispute); Liao, Tr. at 1415:25-1416:4,1416:9-13; RX-235 at 7:38-44. 

533 RX-235 at 15:2-16-3. 

534 See RX- 197 at 8-9. 

106 
in the inventors’ preferred strain WC80-196S.535 Because the deposit does not reflect the best mode 

practiced by the inventors, the deposit in and of itself cannot satisfl the best mode requirement. Nor, 

as Ajinomoto contends, can the deposited strain be considered a satisfactory disclosure of the 

inventors’ preferred lysC replacement step. While it is true that the deposited strain WC80-196 was 

in fact created using the preferred lysC replacement step, the deposit cannot cure the incomplete and 

misleading description of its creation in the ‘698 patent. The inventors purported to give a detailed 

explanation of their best mode in both words and in an allegedly matching deposit. The undersigned 

finds the mismatch between the deposit and the misleading description in the patent effectively results 

in concealment. Nothing in the patent would signal one of skill in the art that the deposit is anything 

other than what was described. Thus, the undersigned finds the ‘698 patent disclosure insufficient 

to enable one of ordinary skill in the art to practice the inventors’ preferred embodiment of the . 

invention as claimed in claim 15 of the ‘698 patent, viz., the WC80-196s host strain with the ldc 

knockout . 

For the reasons discussed herein, the undersigned finds Ajinomoto’s concealment of its 

preferred embodiment of claim 15 of the ‘698 patent to be a violation of the best mode requirement. 

Accordingly, the undersigned finds claim 15 of the ‘698 patent invalid under 35 U.S.C 3 112. 

b. The Ajinomoto inventors failed to disclose their preferred carbon source 

GBT argues that as of the effective filing date of the ‘698 patent, Ajinomoto had a preference 

for sucrose as the carbon source for culturing the claimed micro~rganism.~~~ GBT further argues that 

Ajinomoto inserted sucrose utilization genes into its preferred host strain and usually used sucrose 

535 Kikuchi, Tr. at 718-19. 

536 RIB at 52. 

107 
for their experimental work.537 GBT asserts that Ajinomoto failed to disclose its preference for 

sucrose and thus violated the best mode requirement.538 Specifically, GBT argues that the ‘698 patent 

does not reveal that sucrose may be used as a carbon source, but instead discloses numerous other 

carbon sources, including glucose, lactose, galactose, fructose, and starch hydrolysate.539 GBT argues 

that the specification does not inform a person of ordinary skill in the art that sucrose could be used 

as the carbon source with the only host strain described in the patent.540 

Like GBT, the Staff also argues that Ajinomoto failed to disclose its preference for using 

sucrose as a carbon source and thus violated the best mode requirement of 35 U.S.C. 6 112.541 

Specifically, the Staff argues that the W3 1 10 strain that the inventors used to create the allegedly 

preferred strain described in the ‘698 patent was known not to be able to naturally utilize sucrose.542 

According to the Staff, the specification only states that “[a]s the carbon source, it is possible to use 

sugars such as glucose, lactose, galactose, fructose, and starch hydrolysate; alcohols such as glycerol 

and sorbitol; and organic acids such as fumaric acid, citric acid, and succinic Additionally, 

the Staff argues that sucrose was used as the carbon source in the experiment that forms the basis of 

Example 2 of the ‘698 patent although the specification states that glucose was the carbon source and 

does not disclose that sucrose was used in the experiments.544 Further, the Staff argues that the 

evidence demonstrates that the Aj inomoto inventors added the sucrose utilization genes to increase 

537 Id. 

538 Id. 

539 Id. 

540 Id. 

541 SIB at 59. 

542 Id. 

543 Id. 

544 Id. 

108 
the lysine productivity of the bacteria because sucrose is a more efficient carbon source than 

glucose.545 On this point, the Staff argues that the Ajinomoto research department reported that 

sucrose may be better than glucose for the production of amino acids in E.coli and that lysine yields 

were higher when sucrose was used as the carbon source.546 The Staff also asserts that Kikuchi 

generally used sucrose as the carbon source during his experiments.547 The Staff further asserts that 

increasing productivity through sucrose utilization was one of the three goals set by Kojima at the 

time he became project leader in April 1993 and continued to be a goal throughout the term of the 

Lysine 

Ajinomoto argues that there is no best mode violation for not mentioning sucrose in the ‘698 

patent.549 Ajinomoto argues specifically that all the experts agreed that at the time of filing one skilled 

in the art would know sucrose could be used as a carbon source for E.coli simply by adding a sucrose 

utilization gene.’” According to Ajinomoto, GBT’s case essentially boils down to “sucrose is 

suspiciously missing from the ‘698 Patent, and it might give a 5% higher yield, therefore, the 

inventors cannot be believed.”551 On this point, Ajinomoto argues without citation that while 

theoretically sucrose may give 5% higher yield, that does not make it better.552 Ajinomoto asserts 

that Kikuchi testified that he believed that the choice of sugar sources had nothing to do with the 

545 Id. 

546 Id. at 6 1. 

547 Id. 

548 Id. at 59-60. 

549 CIB at 31. 

550 Id. 

551 Id. at 32. 

552 Id. 

109 
claimed invention.553 Ajinomoto also asserts that while all E.coli use glucose, only some E.coli use 

sucrose.554 Additionally, Aj inomoto asserts that Aj inomoto used glucose almost exclusively. Further, 

noting that the sentence in the specification of the ‘698 patent stating that “[als the carbon source, it 

is possible to use sugars such as glucose, lactose, galactose, fi-uctose, and starch hydrolysate; alcohols 

such as glycerol and sorbitol; and organic acids such as fumaric acid, citric acid, and succinic acid” 

is also in the ‘160 patent specification, Ajinomoto insinuates that the reason the ‘698 patent 

specification does not mention sucrose as a potential carbon source was because it was just stock 

wording added by a patent prosecutor.555 

As previously stated, the best mode analysis is constrained by the scope of the claimed 

invention. Thus, with regard GBT and the Staffs assertion that Ajinomoto’s failure to disclose 

sucrose as a carbon source in the ‘698 patent is a best mode violation, the undersigned must consider 

at the outset whether Ajinomoto failure to disclose their alleged best carbon source is within the scope 

of the claimed invention. Turning first to the claims, the undersigned finds nothing in asserted claim 

15 that would indicate that the inventors were trying to claim the carbon source as part of the 

invention.556 Further, the undersigned finds nothing in the specification to support such a notion. 

Thus, the undersigned finds that “carbon source” is outside the claimed invention of claim 15 of the 

‘698 patent. Although “carbon source” is an unclaimed element, that does not end the best mode 

inquiry. The Federal Circuit has held that unclaimed subject matter may still have to be disclosed in 

some instances to satisfl the best mode requirement if the unclaimed matter “materially affects the 

553 Id. 

554 Id. 

555 Id. at 33. 

556 See JX-2 at 32:47-48. 

110 
properties of the claimed invention.”557 In this instance the record is clear that to cultivate E.coli for 

lysine production the bacteria must be grown in a culture that includes a carbon source.558 Thus, 

because the scope of the claimed invention includes the cultivation of lysine, the undersigned finds 

that a carbon source is necessary to practice the claimed invention. Additionally, the evidence 

suggests that using sucrose improves lysine yields.559 Accordingly, the undersigned finds that under 

the Federal Circuit’s best mode jurisprudence if the Ajinomoto inventors had a preferred carbon 

source, they would be required to disclose it. 

The first step in the best mode analysis is to determine whether the Ajinomoto inventors had 

a subjective preference for a particular carbon source. The undersigned has previously found, supra, 

that the inventors’ preferred host strain (i.e. microorganism) is the strain denominated WC80-196s. 

This strain includes sucrose utilization genes that allow the bacteria to utilize sucrose as a carbon 

source. The inventors’ intentional insertion of the sucrose utilization genes in their preferred host 

strain is strong evidence that the inventors had a preference for sucrose as the carbon source. 

Moreover, it is undisputed that one of the goals of the Lysine Project as of April 1993 was to 

“[ilmprove productivity from sucrose-based raw This fact was reaffirmed by the 

inventors in Research Report No. 14, where the inventors wrote that one of the objectives of their 

research was “[t]o breed high-yield bacteria from su~rose.’’~~’ Also, inventor Kikuchi admitted at the 

557 Bayer AG v. Schein Pharmaceuticals. Inc., 301 F.3d 1306, 1319 (Fed. Cir. 2002). 

558 RFF 3.13 (no dispute). 

559 See CX-234CT (Kikuchi WS) at 7 85. 

560 See JX-38CT at AHL430779; RX-89C (Webb WS) at 7 249; see also RFF 3.47 (no 

561 JX-81CT at AHL433698; Kikuchi, Tr. at 653:ll-18; RX-89C at 7 253. 

dispute). 

111 
hearing that one of the goals of the Lysine Project was in fact to use sucrose as a carbon source.562 

Additionally, the evidence ofrecord shows that once the Ajinomoto researchers had added the sucrose 

utilization genes to WC80-196 to create their preferred host strain WC80-196S, the researchers 

thereafter generally used sucrose for their experimental work.563 Further, in Research Report No. 1 1, 

the inventors provide a reason why sucrose would be their preferred carbon source stating that “[ilt 

is important to fulfill our needs of using cost-saving materials such as sucrose and running a highly 

productive operation in order to beat our competitors such as ADM Corporation.”564 Accordingly, 

for the reasons discussed above, the undersigned finds that the evidence of record clearly shows that 

the Ajinomoto inventors had a subjective preference for using sucrose as the carbon source in 

practicing asserted claim 15, as of the December 1994 effective filing date of the ‘698 patent. 

Having found that the inventors had a subjective preference for sucrose as their carbon source 

in practicing claim 15 of the ‘698 patent, the second part of the best mode inquiry asks whether the 

‘698 patent disclosure would enable one of skill in the art at the time of the invention to practice the 

inventors’ best mode. The specification of the ‘698 patent states “[a]s the carbon source, it is possible 

to use sugars such as glucose, lactose, galactose, fructose, and starch hydrolysate; alcohols such as 

glycerol and sorbitol; and organic acids such as fumaric acid, citric acid, and succinic 

Notably, this rather extensive list does not include sucrose. Ajinomoto argues that the reason the 

above quoted language does not list sucrose is simply because it was “stock language” used by its 

patent counsel. However, that argument is irrelevant to this facet of the best mode inquiry as the 

562 

563 

564 

565 

Kikuchi, Tr. at 652:16-23. 

See Kikuchi, Tr. at 664:24-665:9; CX-234CT (Kikuchi WS) at 7 88. 

JX-98CT at AHL436062. 

JX-2 at 6:47-5 1. 

112 
second part of the best mode analysis focuses on whether objectively the patent disclosure would 

enable one of skill in the art at the time to practice the inventors’ best mode of the claimed invention. 

Because one of ordinary skill would only be aware that the specification does not disclose sucrose, 

Ajinomoto’s reasons for why sucrose is not disclosed are irrelevant. 

According to the evidence of record, it is undisputed that the patent does not mention 

sucrose.566 It is also undisputed that the ‘698 patent does not disclose the introduction of the sucrose 

utilization genes.567 Additionally, the evidence of record establishes that strain W3 1 10, the parent 

strain from which the preferred host strain WC80-196s was created, is known to those of skill in the 

art not to be able to naturally use sucrose as a carbon source.568 

Ajinomoto argues that there is no best mode violation for not mentioning sucrose in the ‘698 

patent, because at the time of filing, one skilled in the art would know sucrose could be used as a 

carbon source for E.coli by adding a sucrose utilization gene. While the record supports Ajinomoto’s 

assertion regarding the knowledge of one of ordinary skill at the time of the filing, the argument is 

irrelevant to the current best mode inquiry. The allegation by GBT and the Staff is that the Ajinomoto 

inventors failed to disclose sucrose as their preferred carbon source for practicing claim 15 ofthe ‘698 

patent. Thus, even if one or ordinary skill in the art at the time would know sucrose could be used 

as a carbon source for E.coli by adding a sucrose utilization gene, that fact would not remedy the 

failing of the ‘698 patent disclosure to inform one of ordinary skill in the art of the inventors’ 

566 RFF 3.17 (no dispute); RFF 3.18 (no dispute)(“Dr. Kikuchi admitted that the use of 

sucrose is not mentioned anywhere in the ‘698 patent even though the patent lists several other 

carbon sources.”). 

567 RFF 3.75 (no dispute). 

568 See Kikuchi, Tr. at 650:4-6; RX-89C (Webb WS) at 7 247; see also Kikuchi, Tr. at 

6 14120-25. 

113 
preference for sucrose. From the evidence discussed above, it is clear that the ‘698 patent fails to 

disclose sucrose, and more specifically the inventors’ preference for sucrose as the carbon source for 

practicing claim 15.569 Thus, the undersigned finds that the ‘698 patent would not enable one of 

ordinary skill in the art as of effective filing date of December 9, 1994 to practice the inventors’ 

preferred embodiment ofthe invention, viz., cultivation of lysine produced using the WC80- 196s host 

strain with the ldc knockout and sucrose as the carbon source. 

For the reasons discussed hereinabove, the undersigned finds Aj inornoto’s concealment of its 

preferred carbon source, sucrose, to be a violation of the best mode requirement. Accordingly, the 

undersigned finds claim 15 of the ‘698 patent invalid under 35 U.S.C fj 112. 

C. The disclosed best mode was fictitious 

GBT argues that the inventors did not actually perform the lysine-production experiments 

described in the ‘698 patent with the disclosed strains and thus the examples in the patent are 

fictitious and invalid under 35 U.S.C. fj 1 12.570 Specifically, GBT argues that Table 1 of the ‘698 

patent purports to reflect the best mode of practicing claim 15, but the evidence establishes that the 

AEC strain on which the experiment supposedly was performed never existed.571 On this point, GBT 

argues that the NTG/AEC-resistance step used in creating the inventors preferred host strain, WC8 1 - 

196S, was done only on strains that had already undergone the mutant lysC replacement and thus, the 

experiments reported in Table 1 were not performed with the described GBT also argues 

that when Ajinomoto was asked to identify the laboratory notebook or other source of the data set 

569 See e.g., RX-89C (Webb WS) at 269. 

570 RIB at 53. 

571 Id. 

572 Id. at 53-54. 

114 
forth in Table 1, Ajinomoto was unable to do so.573 Further, GBT argues that in response to 

interrogatory questions, Aj inomoto pointed to documents that establish that the experiment reported 

in Figure 3 of the ‘698 patent was carried out with different strains and a different carbon source from 

those disclosed in the patent.574 According to GBT, the monthly report from September 1994 contains 

a graph that is identical to the data for the corresponding time points in Figure 3 of the patent, but the 

tested strains are derivatives of the actual best mode host strain.575 Additionally, GBT asserts that the 

experiment used to create the graph in the September 1994 report was done using sucrose as the 

medium, not glucose as disclosed in the ‘698 patent.576 GBT further asserts that Kikuchi’s lab 

notebook contains a table with data identical to the data for the corresponding time points in Figure 

3.577 In contrast to what is disclosed in the ‘698 patent, GBT argues that the experiments in Kikuchi’s 

lab notebook were carried out using a derivative of the best mode strain, WC80-196s using sucrose 

as the carbon source.578 

The Staff, like GBT, argues that claim 15 of the ‘698 patent is invalid because the examples 

disclosed in the ‘698 patent are Specifically, the Staff argues that the experiments 

reflected in Example 3 of the ‘698 patent were actually performed using a bacteria having a different 

genotype than that which is described in the Example.580 Additionally, the Staff asserts that the 

description of Example 3 does not disclose that the actual carbon source used in the underlying 

573 Id. at 54. 

574 Id. 

575 Id. 

576 Id. 

577 Id. at 55. 

578 Id. 

579 SIB at 62. 

Id. at 62-63. 

115 
experiments was sucrose.581 Further, even if the experiments reflected in Examples 3 were run using 

glucose as the carbon source, the Staff argues the examples are nevertheless fictitious because the 

experiments were run using a different strain than that described in the ‘698 patent.582 

Ajinomoto argues that GBT’s argument of fictitious data amounts to little more than “if 

Ajinomoto did not retain the underlying data, then it must be fabricated.”583 According to Ajinomoto, 

many of Ajinomoto’s records, which were written fifteen years ago, no longer Specifically, 

Ajinomoto asserts that Japan has a first to file patent system and that under that system documents 

underlying an invention served no purpose to establish priority and thus at the time of the effective 

filing date of the ‘698 patent, Ajinomoto did not require its inventors to keep their laboratory 

notebooks and allowed them to maintain them or dispose of them as they saw fit.585 Ajinomoto 

asserts that it was not until 1996 that Ajinomoto changed its retention policy.586 With regard to the 

‘698 patent specifically, Ajinomoto argues that Kikuchi testified that he did generate the data in the 

tables in the‘698 patent specification, that the data was on his MacIntosh computer, and that he did 

not save the data when he upgraded to a Windows ~ystem.”~ Ajinomoto asserts that under 

Ajinomoto’s retention policy, Kikuchi had no reason to retain the data.588 Ajinomoto also argues that 

GBT’s assertion that the Figure 3 data is fictitous because it was based on experiments that used 

glucose and the curve in Figure 3 looks like the curve in a figure in Kikuchi’s lab notebook that was 

581 Id. at 63. 

582 Id. 

583 CIB at 37. 

584 Id. 

585 Id. 

586 Id. 

587 Id. at 39. 

588 Id. 

116 
based on sucrose is incorrect because Kikuchi explained that he would expect the curves to look the 

same regardless of the carbon source.589 Additionally, Ajinomoto argues in response to GBT’s 

assertion that the WC196 strain described in the patent never existed that Kikuchi and Liao testified 

that WC 196 was just an abbreviated name of WC80-1 96S.590 

Under the heading “BEST MODE FOR CARRYING OUT THE INVENTION,” the ‘698 

patent states that “[t] he present invention will be more specifically explained ‘below with reference 

to Examples.”591 Example 1 of the patent discloses knocking out the ldc gene from WC 196 to create 

a strain WC 196L, knocking out the cadA gene from WC 196 to create a strain called WC 196C, and 

knocking out the cadA gene from WC196L to create the strain WC196LC.592 Example 2 of the ‘698 

patent discloses the confirmation of L-lysine-decomposing activities of WC 196, WC 196C, WC 196L, 

and WC196LC strains and provides results showing the accumulation of L-lysine and the 

accumulation of cadaverine as a decomposition product of L-ly~ine.~~~ Table 1 purports to show the 

amounts of lysine and cadaverine produced and accumulated using strains WC196, WC196C, 

WC 196L, and WC1 96LC.594 The ‘698 patent describes the results reported in Table 1, and by virtue 

thereof the purported benefit of the claimed invention, stating: 

The accumulation of lysine was increased and the accumulation of cadaverine as a 

decomposition product of lysine was decreased in the WC 196C strain with destruction 

of the cadA gene as compared with WC196 strain, and in WC196L strain with 

destroyed function of the novel lysine decarboxylase gene as compared with WC 196 

and WC196C strains. The accumulation of lysine was further increased, and the 

accumulation of cadaverine as a decomposition product of lysine was not detected in 

589 Id. 

590 Id. 

591 JX-2 at 7: 17-21. 

592 RFF 3.10 (no dispute). 

593 See CRRFF 3.12-1; JX-2 at 9:63-10:60. 

594 JX-2 at Table 1. 

117 
WC 196LC strain with destroyed function of the both lysine decarboxylase genes.595 

Although Example 1 discloses that strains WC 196L and WC 196LC both have the ldc gene knocked 

out, inventor Kikuchi admitted at the hearing that strain WC80-196s and its derivatives were the only 

strains from which the ldc gene had been knocked Because according to Kikuchi strain WCSO196s and its derivatives were the only strains from which the ldc gene had been knocked out, strains 

WCl96L and WC 196LC disclosed in the ‘698 patent, must be fictitious. Thus, the results shown in 

Table 1 must also be fictitious. 

Ajinomoto asserts that WC196 is the same as WC80-196S, arguing that “WC196 . . . is the 

same as the strain WC80-196s used to generate some of the ’698 patent data except for the presence 

of prior art sucrose utilization genes.”597 However, while Ajinomoto argues that WC196 is the same 

as WC80-196S, in the same breath Ajinomoto admits that the two strains are different because strain 

WC 196 admittedly does not include the sucrose utilization genes undisputedly incorporated in the 

WC80-196s strain. Additionally, as described in the ‘698 patent, strain WC196 also lacks the mutant 

lysC gene undisputedly found in strain WC80-196s. Further, while Kikuchi alleges that WC 196 is 

really shorthand for WC80-196S, none of the meticulously kept monthly reports or research reports 

dated prior to the effective filing date of the ‘698 patent on December 9,1994, refers to WC80-196s 

as WC196.598 

Accordingly, for the reasons discussed above, the undersigned finds that the evidence of 

record clearly and convincingly shows that Table 1, and the data presented therein, is fictitious. The 

595 Id. at 10:40-60. 

596 Kikuchi, Tr. at 702: 17-2 1 (emphasis added); see also SFF 443 (no dispute). 

597 See CRRFF 3.98. 

598 See, e.g., JX-43CT; JX-5 1 CT. 

118 
Federal Circuit has held that the disclosure of fictitious data in support of a best mode disclosure in 

a patent is a violation of the best mode requirement of Section 1 lZ5” Thus, the undersigned finds 

claim 15 of the ‘698 patent invalid under 35 U.S.C. $1 12. 

3. Obviousness 

GBT argues that claim 15 of the ‘698 patent would have been obvious to one of ordinary skill 

in the art as of its effective filing date of December 9, 1994.600 According to GBT, clear and 

convincing evidence, including the admissions of one of the inventors, shows that the existence of 

a second lysine decarboxylase was known as of December 1994.601 Knowing that the gene existed, 

GBT argues that a “skilled researcher who wished to do so” would have been able to isolate the gene 

and knock it out using routine techniques.602 GBT argues that techniques for lysine production and 

accumulation were also known, as was the use of E.~oli.~O~ GBT thus argues that every aspect of 

claims 3, 13 and 15 was known, and claim 15 is 

More specifically, with regard to the limitation of claim 3 requiring “wherein the 

microorganism contains a mutant . . . lysine decarboxylase [and] lacks the wild-type gene . . . [and] 

the wild-type lysine decarboxylase comprises the amino acid sequence of SEQ ID NO: 4” GBT argues 

599 See, e.g. Hoffmann-La Roche, Inc. v. Promega Corp., 323 F.3d 1354, 1367 (Fed. Cir. 

2003); Consolidated Aluminum Corp. v. Fonseca Int ’I Ltd., 91 0 F.2d 804, 808 (Fed. Cir. 1990); 

Certain Salinomycin Biomass and Preparations Containing Same, Inv. No. 337-TA-370, Pub. No. 

2978, ID at 46-47 (July 1996), urd sub nom. Kaken Pharm. Co. v. Int ’1 Trade Comm ’n., 1 1 1 F.3d 

143 (Fed. Cir. 1997) (“Salinomycin”). 

6oo RIB at 58. 

601 Id. 

602 Id. 

603 Id. 

604 Id. 

119 
that by December 1994, researchers knew that the claimed wild-type lysine decarboxlyase existed.605 

GBT Wher argues that knowing the existance of the the claimed decarboxlase researchers would 

also be able to discern the gene encoding it.606 On this point GBT asserts that Kojima reported at the 

outset of the Lysine Project that “there are at least two Lys decarboxylases, a major one and a minor 

GBT also relies on a 1980 article from Goldemberg and a 1983 article from Wertheimer and 

Leifer in support of its assertion that that the claimed lysine decarboxylase was known to researchers 

in December 1 994.608 GBT argues in the alternative that even if the existence of the ldc gene was not 

clearly known, given there was strong evidence that a gene encoding the claimed lysine decarboxlyase 

enzyme did exist, it would have been “obvious to try” to isolate the gene.609 Further, GBT asserts that 

one trying to isolate the gene “would certainly have found it.”610 GBT argues that once the claimed 

decarboxlase was found,creating a mutant gene that would not encode a functioning enzyme or 

alternatively, a mutant gene that would reduce its activity or expression, would be routine.611 GBT 

asserts that Ajinomoto expert Liao agreed that the ability to knock out a known gene was known in 

the art6” 

Like GBT, the Staff also argues that claim 15 of the ‘698 patent would have been obvious to 

one of ordinary skill as of the patent’s effective filing date of December 9,l 994.613 Specifically, the 

Staff argues that the evidence demonstrates that the inventors of the ‘698 patent merely applied 

605 Id. at 59. 

606 Id. 

607 Id. 

608 Id. at 59-60. 

609 Id. 

610 Id. 

611 Id. at 62-63. 

Id. at 63. 

613 SIB at 63. 

120 
known techniques to identifj a gene that was believed to exist, and used well known and widely-used 

techniques to neutralize the gene's effects in order to obtain the mutated bacteria covered by claim 

3, on which claim 15 depends.'I4 In support of its argument that the claimed decarboxlyase was 

believed to exist, the Staff, like GBT, relies on the 1980 article by Goldemberg and the 1983 article 

by Wertheimer and Leifer.'I5 The Staff also relies on the statement by Kojima that "[tlhere are at least 

two Lys decarboxylases, a major one and minor one.""' Additionally, the Staff cites to'the testimony 

of GBT's expert, Webb, who states that amino acid decarboxylases generally come in pairs in many 

types of bacteria, that two decarboxylases have been demonstrated with respect to lysine in bacteria 

of the genus Hafnia and Selenomonas, and that E.coli was known to have two decarboxylase genes 

with respect to other amino The Staff argues that the specification makes clear that one of 

ordinary skill would have been interested in discovering whether or not E.coli bacteria had the 

claimed decarboxylase gene, because the specification states that two genes were believed to be 

involved in the decarboxylasion of lysine and that only one had been found .'I8 The Staff further 

argues that Kikuchi's testimony provides the motivation to discover the ldc gene at the time of the 

in~ention."~ Specifically, the Staff refers to the testimony of Kikuchi, where he states: 

[Blut there was a movement underway, globally speaking, to sequence the entire 

genome, not just for E. coli but for different organisms. And so there was, in my 

mind, the notion that prior to my discovery of the gene the lysine decarboxylase gene 

itself, that someone may come out with the sequence for that. And therefore, I think 

I was feeling that I wanted to perform the knockout and see what that knockout would 

have physiologically, so I think I wanted to see quickly what the physiological effect 

'I4 Id. 

'I5 Id. at 63-64. 

'" Id. at 63. 

'I7 Id. at 64. 

'I8 Id. 

'I9 Id. at 64-65. 

121 
of that knockout would be.620 

Ajinomoto argues that claim 15 of the ‘698 patent is valid and nonobvious.621 Ajinomoto 

asserts that the invention of claim 15 of the ‘698 patent covers a method for producing lysine by use 

of E.coli having reduced lysine degradation activity resulting from a mutation to or deletion of the 

ldc gene.622 According to Ajinomoto, there is no dispute that the inventors were the first to produce 

lysine using the novel method and were the first to cultivate microorganisms having a mutated ldc 

gene as described in claim 3, fiom which claim 15 is depends.623 Ajinomoto also argues that as of 

the December 9,1994 effective filing date of the ‘698 patent, a second lysine decarboxylase gene had 

not been isolated or characterized, nor was the sequence Additionally, Ajinomoto argues 

that it is impossible to engineer the wild-type gene out of a strain without first knowing the sequence 

of the gene, and “knowledge of the sequence encoding an enyzme is not a trivial step from merely 

suspecting the existence of an enzyme.”625 Because the ldc gene required by claim 15 had never been 

isolated or sequenced, Ajinomoto argues that the prior art could not show a mutation or deletion of 

the ldc gene.626 Ajinomoto also asserts that GBT’s expert agreed that Ajinomoto was the first to 

isolate and sequence the ldc gene and the first to describe and possess the ldc Further, 

Ajinomoto argues that there is no evidence in the record of any specific motivation for one skilled in 

the art to combine or modify the disclosures of the multitude of prior art references relied upon by 

620 Id. at 65. 

621 CIB at 62. 

622 Id. 

623 Id. 

624 Id. 

625 Id. 

626 Id. 

627 Id. 

122 
GBT to be able to: (1) obtain an Escherichia coli having the ldc knockout gene described in claim 3 

of the ‘698 patent; or (2) use such a microorganism to produce lysine using the method recited in 

asserted claim 1 5.628 

More specifically, Ajinomoto argues that GBT’s experts Somerville and Webb ignore the 

evidence of record that there was considerable uncertainty as of the effective filing date of the ‘698 

patent to the existence of a second lysine decarboxylase gene.629 Additionally, Ajinomoto argues that 

GBT has failed to provide any motivation as to why one of ordinary skill in the art would combine 

the prior art in the way GBT suggests to choose only those specific techniques necessary to produce 

the claimed invention.630 

The determination of obviousness is a question of law based on underlying factual inquiries 

into the (1) the scope and content of the prior art, (2) the level of ordinary skill in the art, (3) the 

differences between the claimed invention and the prior art ; and (4) secondary considerations of nonobviousness (also known as “objective evidence”). The undersigned has determined, supra, that a 

person of ordinary skill in the art to which the ‘698 patent pertains would have an advanced degree 

in Biology, Biochemistry, Genetics, Genomics, Microbiology, Molecular Biology, Agricultural 

Engineering, or Metabolic Engineering with 3-5 years of experience in a laboratory specializing in 

genetic engineering. The undersigned also found, supra, that persons with a Bachelor’s degree could 

also be skilled in the art, but only after on-the-job training under the direct supervision of a Ph.D.- 

level 

628 Id. at 62-63. 

629 Id. at 63. 

630 Id. 

631 See supra, at 1V.D. 1. 

123 
As of December 1994, the effective filing date for claim 15 of the ‘698 patent, the evidence 

of record shows that fermentation was already being used to produce lysine and thus, one of ordinary 

skill in the art at the time would know that fermentation could be used for the production and 

accumulation of lysine.632 The record shows that the cultivation of lysine produced by fermentation 

was also known. Additionally, as discussed in more detail previously with regard to the ‘ 160 patent, 

the evidence shows that one of ordinary skill at the time would know generally that E.coli could be 

used to produce lysine. 

The prior art also includes a 1980 article by Goldemberg titled “Lysine Decarboxylase 

Mutants of Escherichia coli: Evidence for Two Enzyme Goldemberg stated in the article 

that her observations were “consistent with the existence of two kinds of lysine decarboxylase: an 

inducible form, and . . . a constitutive enzyme, thermosensitive and present in very small amounts in 

the three strains compared in this However, contrary to GBT and the Staffs assertion that 

Goldemberg’s work constitutes proof that a second form of lysine decarboxylase existed that was 

distinct fiom the inducible form, the undersigned finds Goldemberg did not conclusively demonstrate 

that the observed lysine decarboxylase activity was caused by a gene other than inducible lysine 

632 See RX-88C (Somerville WS) at 7 33; see also CX-23 1 C (Liao WS) at f 46-47; JX-1 at 

633 See JX-126. 

634 JX- 126 at 2. There are two forms of lysine decarboxylases: the constitutive form and the 

inducible form. RFF 3.21 1 (no dispute). Constitutive and inducible lysine decarboxylases differ in 

amino acid sequence, conditions under which they catalyze the decomposition of lysine, and 

conditions under which each one is formed. RFF 3.2 12 (no dispute). Inducible lysine decarboxylase 

is formed only when cells are cultivated in rich medium, with limited available oxygen, at acidic pH. 

RFF 3.2 13 (no dispute). Constitutive lysine decarboxylase is formed under all conditions of growth. 

RFF 3.2 14 (no dispute). When cells are cultivated in the presence of excess oxygen, at neutral pH, 

the constitutive lysine decarboxylase is the only one formed. RFF 3.21 5 (no dispute). The ldc gene 

encodes the constitutive form of lysine decarboxylase. RFF 3.221 (no dispute). 

1112-13. 

124 
decarboxylase. Goldemberg admits only that the observed lysine decarboxylase activity “might imply 

the existence of at least two enzymes.”635 

In 1983 a prior art article by Wertheimer and Leifer was published with the title, “Putrescine 

and Spermidine Sensitivity of Lysine Decarboxylase in Escherichia coli: Evidence for A Constitutive 

Enzyme . . .”636 While Ajinomoto’s expert Liao agreed that the title of the article suggested that there 

was a constitutive lysine decarboxylase, Liao testified that the activity Wertheimer and Leifer 

observed could have been produced by ornithine de~arboxylase.~~~ Thus, while the article may 

suggest the existence of a constitutive lysine decarboxylase, the evidence does not support the 

conclusion that such a decarboxylase actually existed. 

Also in 1983, a reference by Kamio & Terawaki reported the existence of a constitutive and 

inducible lysine decarboxylase in bacteria belonging to the genus Selenomonas. A 1986 prior art 

reference to Fecker et al. also reported the existence of a constitutive and inducible lysine 

decarboxylase, but in bacteria belonging to the genus Haf~~ia.~~’ Additionally, in a 1986 prior art 

article, Igarashi et al. observed two separate lysine decarboxylase activities, but the second observed 

lysine decarboxylase activity appears to be attributed to ornithine decarboxylase and not a constitutive 

form of lysine decarb~xylase.~~~ Further, a 1985 prior art article by Tabor & Tabor discussed the fact 

that both ornithine and arginine decarboxylases exist in both inducible and constitutive forms in E. 

635 

636 

637 

638 

639 

640 

JX-126 at 2 (emphasis added). 

Liao, Tr. at 1464:24-1465:3. 

See JX-144; JX-138; RX-89C (Webb WS) at 77 357-359. 

JX-132 at 6. 

RX-160; see also RX-89C (Webb WS) at 7 360-361. 

JX-125. 

125 
In addition to that which is cited above, the record evidence shows that as of the December 

1994 effective filing date of the '698 patent, the following techniques were known and available to 

researchers for performing tasks within molecular biology: PCR, the use of endonucleases and ligases 

to create plasmids, mutagenesis through agents like NTG or hydroxylamine, gene sequencing, use of 

multiple copy plasmids to increase gene expression, in vitro mutagenesis of a target gene on a 

plasmid, and AEC selection to identifl feedback desensitized mutants.@' 

What is not disclosed in the prior art, but what is claimed in claim 15 of the'698 patent is an 

Escherichia coli microorganism that lacks the wild-type ldc gene and instead has a mutated ldc gene 

encoding a lysine decarboxylase that has reduced or eliminated activity. Contrary to arguments by 

GBT and the Staff, the record evidence does not support a finding that as of December 1994 a 

constitutive form of lysine decarboxylase in E.coli was known to exist. 

While GBT and the Staff argue that creating such a microorganism would have been obvious 

to one of ordinary skill in the art at the time of the effective filing date of December 1994, the 

evidence of record does not support such a conclusion, especially not clearly and convincingly. 

Moreover, GBT and the Staff incorrectly frame the obviousness inquiry. The invention of claim 15 

is not merely directed to an Escherichia coli strain with the specific mutation recited in claim 3 of the 

'698 patent, but rather a method of producing, accumulating and cultivating lysine. Thus, the proper 

obviousness inquiry is whether one of ordinary skill in the art as of December 9, 1994 would have 

found it obvious to produce lysine using a microorganism of the species Escherichia coli that lacks 

See Liao Tr. at 1424:l-1425:22; see also RX-89C (Webb WS) at 17 306,307,309-12, 

33 1-33,337,339. 

126 
the wild-type ldc gene and instead has a mutant ldc gene.642 

As with regard to the ‘ 160 patent, GBT and the Staff again have used impermissible hindsight 

to conclude that claim 15 of the ‘698 patent was obvious. GBT and the Staffs case for obviousness 

amounts to little more than an argument that because the tools and techniques necessary to create the 

specified mutant ldc gene were available and known to one of ordinary skill in the art in December 

1994, claim 15 must be obvious. The Supreme Court, however, recently reaffirmed the impropriety 

of such an approach, stating that “a patent composed of several elements is not proved obvious merely 

by demonstrating that each of its elements was, independently, known in the prior 

Additionally, GBT argues that given the evidence that the ldc gene existed, it would have been 

“obvious to try” to isolate the gene.644 However, the Federal Circuit has consistently held that 

“obvious to try” is not to be equated with obviousness.645 

GBT argues that it would have been an obvious choice in December 1994 to use E.coli as the 

microorganism for lysine production. However, the evidence shows that there were inherent 

difficulties in using E.coli for lysine fermentation, not the least of which being that E.coli is not a 

natural lysine producer.&16 Moreover, at the time, Corynebacterium was being used almost exclusively 

for the production of ly~ine.~’ Thus, while Ajinomoto may have had a specific motivation as a result 

of the competitive threat from Archer Daniels Midland to begin looking for nonconventional ways 

642 See 35 U.S.C. $103 (A claim is obvious if “the differences between the subject matter 

sought to be patented and the prior art are such that the subject mutter us u whole would have been 

obvious at the time the invention was made to a person having ordinary skill in the art to which said 

subject matter pertains.”)(emphasis added). 

643 KSR, 127 S.Ct. 1727, 1741 (2007). 

644 RIBat62. 

645 See Gillette Co. v. S.C. Johnson & Son, Inc., 919 F.2d 720, 725 (Fed. Cir. 1990). 

646 See CX-234C (Kikuchi WS) at 76; CX-235C (Kojima WS) at 23. 

647 CX-231C (Liao WS) at 7 46,44,48; see also Somerville, Tr. at 1235:9-13. 

127 
to more efficiently produce lysine, there is no evidence that anyone else would have been so 

It is undisputed that the wild type ldc gene whose absence is required by claim 15 of the ’698 

patent had not been isolated or sequenced in the art.649 On this point, the evidence indicates that it 

is impossible to engineer the wild-type gene out of a strain without knowing the sequence ofthe gene, 

and knowledge of the sequence encoding an enzyme is not a trivial step from merely suspecting the 

existence of the ldc enzyme.650 Further, it is undisputed that Ajinomoto was the first to describe the 

ldc knockout and the first to possess the ldc gene with a knockout.65’ The prior art relied on by GBT 

and the Staff does not show that the techniques available at the time of the invention could have been 

used by one of ordinary skill to disclose the ldc gene or to use a mutation of the ldc gene. As is 

typical when impermissibly relying on hindsight to conclude obviousness, GBT and the Staff fail to 

provide any reason why one of ordinary skill in the art at the time would have combined or modified 

the many prior art references cited to get to the claimed invention of claim 15 of the ‘698 patent. 

As discussed above, GBT and the Staff use impermissible hindsight to sift through the prior 

art to conclude that claim 15 of the ‘698 patent is obvious. While Webb and Somerville’s pathway 

648 See CX-235C (Kojima WS) at 7 7 (stating that the origin of theLysine Project began “[iln 

1990, [when] Ajinomoto concluded that it was at a competitive disadvantage to Archer Daniels 

Midland (“ADM’) in the production of L-lysine. ADM has access to its own internal glucose 

supplies at a much lower cost than Ajinomoto. Companies like ADM, who have separate sugar 

processing operations, generate huge quantities of glucose that can be used as the raw material to 

make amino acids through fermentation.”), 7 78 (“In order to compete with Archer Daniels Midland, 

we attempted to improve the quality of the bacterial strain that is used in a fermentation process to 

produce lysine. We hoped that we could overcome the cost advantage that Archer Daniels Midland 

had in the raw materials with an improvement in the bacteria used in the fermentation process.”). 

649 CX-23 1C (Liao WS) at 7 203; Somerville, Tr. at 890:13-890:23. 

cx-23 1 C (Liao WS) at f 202. 

651 Somerville, Tr. at 891 :24-892:7. 

128 
to the invention may in retrospect seem to follow logical steps using available tools and techniques 

to come to the invention of claim 15, at the time of the invention the inventor’s insights and 

willingness to confront and overcome obstacles cannot be discounted. Accordingly, for the reasons 

discussed above, the undersigned finds that GBT and the Staff failed to prove by clear and convincing 

evidence that claim 15 of the ‘698 patent was obvious as of the date of the effective filing date of 

December 9, 1994. 

E. Unenforceability - Inequitable Conduct 

GBT and the Staff argue that the ‘698 patent is unenforceable based on the applicants’ 

inequitable conduct.652 Specifically, GBT and the Staff argue that Ajinomoto’s failure to disclose 

their best mode of practicing claim 15 of the ‘698 patent (ie., the WC80-196s strain) and their best 

mode of practicing claim 13 of the ‘698 patent (i.e., the TAML66E strain) are material, because best 

mode is a requirement of patentability.653 Likewise, GBT argues that both the inventors’ failure to 

disclose sucrose as their preferred carbon source and the inventors’ inclusion of fictitious examples 

in the specification supports a finding of inequitable 

GBT asserts that the inventors did not disclose in the ‘698 patent the one strain, WC80-196S, 

they used to practice claim 1 5.655 Instead, GBT asserts the inventors disclosed a fictitious strain that 

made no mention of the lysC replacement and the insertion of sucrose utilization genes that are 

included in preferred strain WC80-1 96S.656 GBT argues that while Ajinomoto’s internal documents 

candidly disclose the lysC replacement and the insertion of sucrose utilization genes, in public 

652 SIB at 68-71; RIB at 63-66. 

653 SIB at 68,69; RIB at 63,65. 

654 RIB at 63-64. 

655 RIB at 63. 

656 Id. 

129 
documents these two steps were concealed.657 GBT and the Staff argue that keeping the two steps a 

secret is strong evidence of an intent to deceive.658 Additionally, with regard to intent, GBT notes that 

while the patent explicitly recites an extensive list of possible carbon sources to practice claim 15 of 

the’698 patent, the list conspicuously does not include sucrose, the inventors preferred carbon 

source.659 GBT asserts that Ajinomoto kept the beneficial effects of sucrose on lysine production as 

a trade secret for over ten years and then filed and received a patent covering that very thing.660 

According to GBT, had the inventors publicly deposited and disclosed WC80-196S, Ajinomoto could 

not have obtained patent protection for the producing lysine using strains with sucrose utilization 

genes because the disclosure in WC80-196s would have anticipated any such patent claims.661 GBT 

argues that the only conclusion to be drawn from Ajinomoto’s actions is that the inventors 

intentionally withheld their preference for sucrose as a carbon source.662 GBT argues that the 

inventors’ conduct evinces a pattern of non-disclosure and misrepresentation. Because the omission 

of information concerning the inventors’ best mode is highly material and there is strong evidence 

of intent, GBT and the Staff argue that the inventors committed inequitable conduct when prosecuting 

the ‘698 patent.663 

Ajinomoto argues that GBT and the Staffs inequitable conduct argument fails both the 

materiality and intent prongs.664 With regard to materiality, Ajinomoto argues that since there was 

657 Id. 

658 Id. ; SIB at 69. 

659 RIB at 64. 

Id. 

Id. 

662 Id. 

663 Id. at 64,66; SIB at 69. 

664 CIB at 45. 

130 
no best mode violation with respect to claim 15 and claim 13, GBT cannot establish materiality.665 

With regard to intent, Ajinomoto asserts that the inventors testified that they did not intend to deceive 

anyone with respect to either sucrose, the lysC replacement, or TAML66E.666 Ajinomoto argues that 

the undersigned was in a position to judge the credibility of the ‘698 inventors and see that GBT’s 

argument is baseless.667 Ajinomoto also asserts that Japan has no best mode requirement, arguing that 

GBT cannot explain how one can have an intent to deceive where there is no opportunity for 

deception.668 

As discussed above, GBT and the Staff argue that the ‘698 patent is unenforceable because 

the patent applicants intentionally failed to disclose their best mode for claims 15 and 13, intentionally 

failed to disclose their preference for sucrose as a carbon source and because the applicants included 

fictitious examples in the patent specification. The undersigned has already determined, supra, that 

the inventors violated the best mode requirement of Section 1 12 with regard to claim 15 for failing 

to disclose their preferred host strain WC80-196s and their preference for sucrose as a carbon source. 

Additionally, the undersigned has found, supra, that the inventors violated the best mode requirement 

by including fictitious examples in the specification allegedly in support of their best mode of 

practicing claim 15 of the ‘698 patent. While the undersigned has not yet adjudicated GBT and the 

Staffs allegation that the inventors also violated the best mode requirement by failing to disclose their 

preferred host strain for practicing claim 13 of the ‘698 patent, the undersigned finds such an exercise 

unnecessary as its previous findings provide ample evidence of inequitable conduct. 

665 Id. 

Id. at 47. 

667 Id. 

Id. 

131 
There can be no doubt based on the evidence of record that the inventors of the ‘698 patent 

knew of the preferred WC80-196s strain as of the effective filing date of December 9, 1994. 

Likewise, there can be no doubt that the inventors were well aware that sucrose could be used as a 

carbon source in the production of lysine using strain WC80-196s. Because disclosure of the best 

mode is statutorily required, the undersigned finds Ajinomoto’s failure to disclose its preference for 

using host strain WC80-196s to practice claim 15 and its failure to disclose its preference for sucrose 

as a carbon source is material. 

With regard to intent, the record evidence shows that Ajinomoto engaged in a pattern of nondisclosure in procuring the ‘698 patent, including the failure to disclose its preferred host strain for 

practicing claim 15 and its preference for sucrose as a carbon source. Moreover, the record evidence 

shows that Ajinomoto made a series of misrepresentations in procuring the ‘698 patent. Specifically, 

the ‘698 patent describes how to create the alleged best mode strain for practicing claim 15, but fails 

to disclose two steps the inventors took in creating their preferred host strain WC80-196S, namely 

the lysC replacement step and the inclusion of sucrose utilization genes. Additionally, while the 

specification explicitly discloses a long list of carbon sources that may be used to practice claim 15, 

the specification conspicuously fails to disclose the inventors’ preferred carbon source, sucrose. The 

specification further conceals the inventors’ preference for sucrose by only disclosing examples in 

support of the best mode disclosure that are based on experiments allegedly run using glucose. By 

failing to disclose both the addition of sucrose utilization genes in its preferred host strain and the use 

of sucrose as a preferred carbon source, the evidence suggests the inventors intended to deceive the 

PTO. Furthermore, the intentional inclusion of fictitious data in Table 1 to support the patentability 

of claim 15 also supports a finding of the requisite intent to deceive. Notably, Ajinomoto’s failure 

132 
to disclose its best lysine producing host strain comes during a time when the record evidence 

indicates Ajinomoto was facing increased business competition from ADM. Ajinomoto’s intentional 

inclusion of fictitious information and data, coupled with its failure to disclose the inventors’ true best 

mode for practicing claim 15 and the inventors’ preference for sucrose as a carbon source, leads the 

undersigned to the inescapable conclusion that Ajinomoto had an intent to deceive when it filed its 

patent application. Because both the materiality and intent elements are high, equity demands a 

finding of inequitable conduct. Accordingly, based upon strong evidence of specific acts of 

concealment and misrepresentation by the applicants in connection with the ‘698 patent, the 

undersigned finds by clear and convincing evidence that the ‘698 patent is unenforceable due to 

inequitable conduct before the PTO. 

VI. Unclean Hands 

GBT argues that Ajinomoto has “engaged in a duplicitous and inherently inequitable scheme 

to bolster its prospects for success in this investigation by misusing for litigation purposes its feigned 

interest in purchasing GBT’s facilities for producing lysine.”669 According to GBT, Aj inomoto has 

“contracted in bad faith, procured commercial information and technology through false pretenses, 

and attempted to conceal and perpetuate this deceitful scheme and maximize its advantage in this 

inve~tigation.”~~’ GBT asserts that Ajinomoto seeks equity from the ITC, but has not behaved 

eq~itably.~~’ 

Ajinomoto argues that GBT’s unclean hands defense should be denied.672 Contrary to GBT’s 

669 RIB at 67. 

670 Id. 

671 Id. 

672 CIB at 69. 

133 
argument, Ajinomoto argues that the evidence shows that Ajinomoto participated in discussions with 

GBT in good faith.673 Specifically, Ajinomoto argues that the significant time, resources and energy 

it devoted to the discussions with GBT, the fact that it did not breach any duty of confidentiality owed 

to GBT in connection with the discussions, and the fact that the discussions failed for reasons 

unrelated to the patent infringement at issue here, demonstrate that Ajinomoto acted in good faith.674 

Ajinomoto asserts that its interactions with GBT, its investigation of GBT’s patent infringement, and 

its initiation of this investigation “were not unconscionable, fraudulent or deceitful conduct justifying 

the application of the unclean hands Ajinomoto argues that GBT has failed to prove a 

nexus between its alleged inequitable conduct and the equity it seeks in this inve~tigation.~~~ In 

particular, Ajinomoto argues that GBT’s unclean hands theory is neither “borne out by the facts nor 

does it establish the required nexus between the validity and enforceability of the patents-in-suit and 

Ajinomoto’s participation in acquisition discussions and its investigation of suspected 

infringement.”677 While GBT argues that it was misconduct for Ajinomoto to test the lysine product 

samples GBT provided during the September 5,2005 plant tour, Ajinomoto argues that the samples 

were of finished lysine products available in the marketplace and thus could not be confidential.678 

Additionally, Ajinomoto asserts that there is no evidence that Ajinomoto’s plant tour was intended 

as anything other than a fact finding mission in pursuit of a potential future business relationship.679 

Further, Ajinomoto argues that there is no evidence that Ajinomoto participated in the plant knowing 

673 Id. at 68. 

674 Id. 

675 Id. 

676 Id. at 70. 

677 Id. 

678 Id. 

679 Id. 

134 
that it intended to pursue litigation against GBT. In fact, Ajinomoto asserts that GBT acknowledges 

that Ajinomoto’s decision to pursue a Section 337 investigation against GBT was made after the 

September 5, 2005 plant tour.680 Ajinomoto also asserts, in contrast to GBT’s allegation that 

Ajinomoto’s consideration of a potential purchase of GBT was a “pure sham,” that it established a 

working group composed of some of its highest executives to study the potential transaction, set a 

budget of $8 million for advisory and legal fees and due diligence, hired JPMorgan as an investment 

advisor, and conducted numerous high-level meetings regarding the viability of a potential 

transaction.681 Ajinomoto notes that it took the above steps after the September 5,2005 plant tour and 

before GBT provided any substantive due diligence information.682 Aj inomoto also argues that GBT’s 

unclean hands theory is barred by the Noerr-Pennington Doctrine.683 Ajinomoto argues that under 

the Noerr-Pennington Doctrine, a patent holder is immune from claims of unfair competition or 

antitrust violation premised upon enforcing patent rights.684 

The Staff also argues that GBT’s unclean hands argument should be rejected.685 Specifically, 

the Staff argues that the factual circumstances surrounding GBT’s allegations of unclean hands are 

unlike those in the decisions GBT cites, where the act complained of bore a direct relationship to the 

cause of action.686 The Staff argues that GBT’s unclean hands defense, which the Staff asserts is 

based on allegedly fraudulent acquisition negotiations, is similar to the allegedly fraudulent settlement 

negotiations that served as the basis of the defendant’s unclean hands defense that was rejected in 

Id. at 70-7 1. 

Id. 

Id. 

683 Id. at 72. 

684 Id. 

685 SIB at 72. 

Id. at 71. 

135 
Sanoji-Synthelabo v. Apotex, Inc., 470 F.3d 1368,1384 (Fed. Cir. 2006).687 The Staff argues that as 

in Sanoji, Ajinomoto’s alleged fraudulent conduct relates to “negotiations” well after the patents were 

obtained and thus GBT’s unclean hands defense should be denied.688 

The unclean hands doctrine provides that a court’s equitable power “can never be exerted on 

behalf of one who has acted fraudulently, or who by deceit or any unfair means has gained an 

advantage.”689 Courts will only apply the doctrine when it has been shown that the inequitable 

conduct bears “an immediate and necessary relation to the equity” that the patent holder seeks in 

litigation.690 Unclean hands must be proven by clear and convincing evidence.691 

The parties have stipulated to the following facts regarding GBT’s defense of unclean hands. 

In September 2004, Ajinomoto received an inquiry from an officer of Nikko Citigroup Limited 

regarding a sale [ 3 8.1 % holdings 

of GBT 3 regarding such possible sale took place in Hong Kong 

in February 2005.693 There was no further direct contact between Ajinomoto and GBT until August 

8,2005, when Ajinomoto, in the context of expressing its interest in the possible acquisition of GBT’s 

lysine operation, wrote GBT requesting a plant visit, expressing understanding for GBT’s sensitivity 

3 of [ 

A meeting with [ 

687 Id. at 72. 

688 Id. 

689 Keystone Driller Co. v. General Excavator Co., 290 U.S. 240,245 (1933). 

690 Certain Home Vacuum Packaging Products, 337-TA-496,2004 WL 1082507, Notice, 

at 88-89 (March 2004); see also Precision Instrument Mfg., Co. v. Automotive Maint. Mach. Co., 

324 U.S. 806,s 15 (1 945). 

691 In re Omeprazole Patent Litigation, 483 F.3d 1364,1374 (Fed. Cir. 2007) (“Andrx bears 

the burden of proving by clear and convincing evidence that Astra acted with unclean hands.”). 

Notably, GBT incorrectly asserts in its post-hearing brief that the standard is preponderance of the 

evidence. See RIB at 69. 

692 JX-191C at 7 1. 

693 Id. at 7 2. 

136 
about trade secrets and offering a confidentiality agreement not to use or disclose any confidential 

information obtained during the visit.694 A confidentiality agreement, dated August 8, 2005, was 

executed by Ajinomoto and delivered to GBT.695 On and after August 24,2005, Ajinomoto, unknown 

to GBT, was testing the L-lysine products of GBT and another manufacturer that were purchased from 

the market to determine whether the microorganism used in producing them were brevibacteria or E. 

On August 25 and 29, 2005, E. coli and brevibacteria DNA were detected in the lysine 

products of GBT.697 On September 5,2005, at Ajinomoto’s request, five employees of Ajinomoto 

visited GBT for a plant tour.698 One of Ajinomoto’s employees took pictures of a GBT facility from 

a highway outside the GBT facility.699 Ajinomoto’s employees visited GBT’s plants for the 

manufacture of L-lysine, including its plant in Dehui, China.700 During the plant tours, Ajinomoto’s 

employees were provided information with respect to GBT’ s L-lysine, including its principal raw 

materials, its auxiliary materials, energy use, production facilities and At Ajinomoto’s 

request, GBT provided Ajinomoto’s representatives with samples of its finished crystalline and 

sulphate L-lysine products during the plant visit.702 On or after September 8, Ajinomoto’s laboratory 

was requested to test the GBT product samples obtained during the GBT plant visit and purchased 

by Ajinomoto for the dapA and ldc genes covered by the ‘160 and ‘698 patents.703 Those tests, in 

694 Id. at fl 3. 

695 Id. at 7 4. 

696 Id. at fl 5. 

697 Id. 

698 Id. at fl 6. 

699 Id. at 7 7. 

700 Id. at 7 8. 

701 Id. at 7 9; see also Rx- 12 1 C. 

702 Id. at fl 10. 

703 Id. at fl 1 1. 

137 
Ajinomoto’s view, confirmed that the dapA and ldc mutations were present.704 On September 22, 

2005, Ajinomoto decided to consult Dr. Labgold at Patton Bogg~.~’~ The issue of initiating an 

investigation under Section 337 was discussed when Ajinomoto representatives met with U.S. counsel 

on or around September 29, 2005.706 By about October 3 1,2005, Heartland had obtained samples of 

GBT’s L-lysine in the United States.707 By October 20,2005, Ajinomoto and Heartland had begun 

preparing for filing a case against GBT “as soon as possible.”708 In late October 2005 Ajinomoto 

continued to conduct analyses of GBT’s L-lysine provided during the GBT plant tour and purchased 

by Ajinomoto from the market for purposes of determining the microorganism used in producing it 

and other qualities.709 On October 3 1,2005, Ajinomoto thanked [ 3 and GBT for the plant 

visit and stated that it wished to pursue “strategic opportunities” with GBT based on “internal 

discussions at both divisional and management levels.”710 A meeting for this purpose in Hong Kong 

was On November 2, 2005, Ajinomoto kicked off its “Gallop Project,” which was 

formed to negotiate with GBT. The Gallop Project team was advised that “[i]nformation disclosed 

in the course of negotiations may be used for purposes of evaluating M&A, and may not be used for 

any other purposes such as, for example, patent litigation (relevant information may not be conveyed 

to members who are assigned to patent litigation).”712 Senior Managing Director Yanagihara was 

704 Id. 

705 Id. 

706 Id. at 7 12. 

707 Id. at 7 13. 

708 Id. at 7 14. 

709 Id. at 7 15. 

710 Id. at 7 16. 

711 Id. 

712 Id. at 7 17. 

138 
assigned to head the team for the Gallop On November 2,2005, [ ] on behalf of 

GBT, agreed to hold a meeting with Ajinomoto in Hong Kong and/or other suitable locations to 

discuss “the potential transa~tion.”~’~ On November 16, 2005, General Manager of Production & 

Technology Administration Center of Ajinomoto, Koji Igarashi, sent an email to Kazuhito Suzuki of 

Ajinomoto USA regarding “PCR analysis in the USA,” of GBT’s L-lysine which stated “this matter 

concerns the fate of the company, and the top management is demanding urgency.”715 Ajinomoto 

continued to have internal discussions about the possibility of a transaction with GBT, and contacts 

between Ajinomoto and GBT relating to negotiations for a potential transaction continued until 

December 20, 2005.716 On December 21,2005, Ajinomoto advised GBT through JPMorgan there 

would be no meeting in Hong Kong and that the discussions had come to an end.717 On January 1 1, 

2006, Heartland’s and Ajinomoto’s counsel discussed with the ITC’s Office of Unfair Import 

Investigations the time and date for a meeting to discuss Section 337 filing procedures and a 

complaint.718 On April 24, 2006, Heartland filed a Complaint with the U.S. International Trade 

Commission under Section 337 charging GBT with patent infringement, and, simultaneously, filed 

a complaint for patent infringement in the U. S. District Court for the District of Delaware.719 The 

decision for Heartland to file a Section 337 complaint with the U.S. International Trade Commission 

was made by Ajin~rnoto.~~’ Prior to the filing of the complaints with the U.S. International Trade 

713 Id. at 7 18. 

714 Id. at 7 19. 

715 Id. at 720. 

716 Id. at721. 

717 Id. at T 22. 

718 Id. at 7 23. 

719 Id. at 7 24. 

720 Id. atT25. 

139 
Commission and the U.S. District Court for the District of Delaware, neither Ajinomoto nor 

Heartland ever advised GBT of their views regarding GBT’s infringement of their L-lysine patents 

or their intention to initiate litigation premised on patent ir~fringement.~~’ 

GBT’s unclean hands argument is devoid of substance and, for the reasons discussed below, 

is rejected. GBT asserts that Ajinomoto acted in bad faith in its dealing with GBT, but provides no 

credible evidence of bad faith.722 Rather GBT simply restates the stipulated facts without explaining 

how those facts relate to its assertion of bad faith.723 The only evidence GBT points to in support of 

its assertion of bad faith is that Ajinomoto failed to tell the people who toured GBT’s plant that there 

was a confidentiality agreement in place.724 However, without more, the undersigned fails to see how 

the mere fact that the people on the plant tour were unaware of the confidentiality agreement evinces 

bad faith on the part of Ajin~moto.~*~ 

GBT also argues that Ajinomoto engaged in inequitable conduct “in misrepresenting to GBT 

that it was dealing as a prospective buyer, while concealing that it was preparing to be an opposing 

party in litigation and was breaching the Confidentiality Agreement.”726 However, GBT provides no 

credible evidence that Ajinomoto was in fact misrepresenting to GBT that is was a prospective buyer. 

After all, GBT does not dispute that a potential joint venture or acquisition of some or all of GBT’s 

amino acid feed division presented several strategic benefits to Ajinomoto, including access to the 

721 Id. at f 26. 

722 See RIB at 69-70. 

723 Id. 

724 Id. 

‘ 725 Notably, while the people on the plant tour may have been unaware of the confidentiality 

agreement, the evidence does show that the group that toured GBT’s facility did discuss that 

“whatever that we would see would not be divulged to outside parties.” See RX-52C (Shiroshita 

Depo.) at 56:2-14. 

726 See RIB at 70. 

140 
large and growing Chinese market.727 Additionally, the evidence shows that it was [ 

3 who initiated discussions in 2004 regarding the sale of 

[ 3 8.1 % holdings in GBT.728 Furthermore, the evidence of record shows that Ajinomoto expended 

considerable resources and energy in Merance of its acquisition negotiations with GBT, thus 

undercutting GBT’s argument that Aj inomoto was misrepresenting itself as a prospective buyer. 

Specifically, the evidence shows that Aj inomoto established a working group comprising high-level 

executives, hired JPMorgan Securities as an investment advisor, established an $8 million budget and 

plan for hiring other advisors and conducting due diligence, and held numerous high-level 

meetings.729 

With regard to GBT’s assertion that there is something inequitable about Ajinomoto 

negotiating with GBT as a prospective buyer while at the same time preparing for litigation against 

GBT, the undersigned finds that without more the mere fact that Ajinomoto was investigating the 

possible acquisition of GBT while at the same time preparing for litigation against GBT is not 

evidence of inequitable conduct or bad faith. As for GBT’s assertion that the plant tour was in 

furtherance of Ajinomoto litigation strategy, GBT acknowledges that Ajinomoto’s decision to pursue 

a Section 337 investigation against GBT was made after the September 5,2005 plant tour.730 

The crux of GBT’s unclean hands argument rests on its assertion that Ajinomoto violated the 

confidentiality agreement when Ajinomoto used the lysine samples provided by GBT in furtherance 

of the acquisition negotiations to prepare for litigation against GBT. Notably, the alleged breach of 

727 CFF 7.8 (no dispute). 

728 See JX-191C at 1; RX-122C. 

729 See RX-137C at 3-4; RX-136C at 4-5; RX-133C at 14. 

730 JX- 19 1 C at 17 1 1, 12; see also RX- 125C. 

141 
the confidentiality agreement is really the only arguably bad act that GBT points to in support of its 

unclean hands defense. The confidentiality agreement defined Confidential Information as: 

All data, reports, interpretations, forecasts and records containing or otherwise 

reflecting information concerning [GBT], its affiliates and subsidiaries that is not 

available to the general public and is disclosed to Ajinomoto by [GBT] in the course 

of its dealings with [GBT] and that is conspicuously specified to be “Confidential” by 

[GBT] in writing prior to 

The evidence of record shows that the lysine samples provided to Ajinomoto were finished lysine 

products that could have been purchased in the marketplace.732 Additionally, GBT fails to provide 

any proof that the samples given to Ajinomoto were marked “Confidential” as required by the 

Confidentiality Agreement. Because the samples given Ajinomoto were publically available and 

there is no evidence that the samples were marked “Confidential,” the undersigned finds that 

Ajinomoto’s use of the lysine samples could not constitute a violation of the confidentiality 

agreement. 

As previously discussed , to prove the defense of unclean hands, the inequitable acts must bear 

an immediate and necessary relation to the equity being sought in litigation. The undersigned has 

found herein that GBT has failed to prove any inequitable act that could form the basis of GBT’s 

unclean hands defense. However, assuming arguendo that the use of the samples provided to 

Ajinomoto in preparation for litigation against GBT is deemed an inequitable act, the evidence still 

does not support a finding of unclean hands, because the breach of the confidentiality agreement has 

no immediate and necessary relation to Ajinomoto’s claim that GBT infringes claim 15 of the ‘160 

patent. 

731 CFF 7.5 (no dispute). 

732 RX-52C (Shiroshito Depo.) at 50:4-5 1 : 17, 171 : 18-1 72:2. 

142 
Accordingly, for the reasons set forth hereinabove, the undersigned finds that GBT has failed 

to prove by clear and convincing evidence its defense of unclean hands. Because the undersigned has 

found against GBT on the issue of unclean hands, the undersigned need not address Ajinomoto’s 

alternative argument that GBT’s unclean hands argument is barred under the Noerr-Penington 

Doctrine. 

VII. Domestic Industry - Economic Prong 

Ajinomoto and GBT stipulate that an industry relating to the production and sale of the amino 

acid L-lysine exists in the United States, that L-lysine is used in a number of products, including 

animal feed additives, and that the domestic industry includes Ajinomoto’s substantial United States 

investment and expenditures in the manufacture of L-lysine products using patented genetic 

constructs and methods as well as distributors for L-lysine products, which includes Ajinomoto’s 

investment in its wholly-owned subsidiary - Heartland.733 Ajinomoto and GBT also stipulate that 

Heartland’s headquarters are located in the United States at 8430 W. Bryn Mawr Avenue, Suite 650, 

Chicago, Illinois. Heartland’s manufacturing/production facilities are located in Eddyville, 

Additionally, Ajinomoto and GBT stipulate that Heartland and Ajinomoto have made 

significant investment in their manufacturing facilities and equipment in the United States relating 

to the manufacture of their L-lysine Specifically, Ajinomoto and GBT stipulate that 

Ajinomoto has substantially invested in its manufacturing facility and equipment at Heartland’s 

Eddyville, Iowa, facility where the relevant L-lysine products are manufactured.736 Ajinomoto and 

733 JX-192C at f 3. 

734 JX- 192C at 7 4. 

735 JX- 192C at f 6. 

736 Id. 

143 
GBT additionally stipulate that Heartland and Aj inomoto have made significant capital investments 

in Heartland’s business infrastructure including, but not limited to, expansion and modification of 

Heartland’s Eddyville, Iowa, plant.737 Further, Ajinomoto and GBT stipulate that Heartland employs 

a significant number of employees in its U.S. L-lysine operations and, in particular, its manufacture 

of L-lysine 

Accordingly, based on the above stipulations, the undersigned finds that Ajinomoto has 

satisfied the economic prong of tHe domestic industry requirement of Section 337.739 

737 Id. at 7 7. 

738 Id. at 7 8. 

739 The Staff acknowledges that the stipulation resolves all issues concerning jurisdiction, 

infringement, and domestic industry. SPHB at 19. 

144 
CONCLUSIONS OF LAW 

1. The Commission has subject matter jurisdiction in this investigation. 

2. The Commission has personal jurisdiction over Respondents Global Bio-Chem Technology 

Group Company Limited, Changchun Dacheng Bio-Chem Engineering Development Co., 

Ltd., Changchun Baocheng Bio-Chem Development Co., Ltd., Changchun Dahe Bio 

Technology Development Co., Ltd., and Bio-Chem Technology (HK) Limited. 

3. Respondents’ manufacture of L-lysine feed products using the Old Escherichia bacterium 

strain deposited with the ATCC under Accession #SD-5590 infringes claim 15 of U.S. Patent 

No. 6,040,160 in violation of 35 U.S.C. 5 271(a). 

Respondents’ manufacture of L-lysine products using the Corynebacterium strain deposited 

with the ATCC under Accession #SD-5620 and the New Escherichia bacterium strain 

deposited with the ATCC under Accession #SD-5717 do not infringe Claim 15 of U.S. Patent 

No. 6,040,160. 

Respondents’ manufacture of L-lysine feed products using the Old Escherichia bacterium 

strain deposited with the ATCC under Accession #SD-5590 infringes claim 15 of U.S. Patent 

4. 

5. 

No. 5,827,698 in violation of 35 U.S.C. 9 271(a). 

Respondents’s manufacture of L-lysine products using the Corynebacterium strain deposited 

with the ATCC under Accession #SD-5620 and the New Escherichia bacterium strain 

deposited with the ATCC under Accession #SD-5717 do not infringe Claim 15 of U.S. Patent 

No. 5,827,698. 

An industry in the United States exists with respect to Ajinomoto’s products that is protected 

by U.S. Patent Nos. 6,040,160 and 5,827,698 as required by 19 U.S.C. 9 1337(a)(2) and (3). 

6. 

7. 

145 
8. Claim 15 0fU.S. Patent No. 6,040,160 is invalid under 35 U.S.C. 5 112 for failing to disclose 

best mode. 

9. Claim 15 of U.S. Patent No. 5,827,698 is invalid under 35 U.S.C. 9 112 for failing to disclose 

best mode. 

Claim 15 of U.S. Patent No. 6,040,160 is not invalid under 35 U.S.C. 0 103 for obviousness. 

Claim 15 of U.S. Patent No. 6,040,160 is not invalid for obviousness-type double patenting. 

Claim 15 of U.S. Patent No. 5,827,698 is not invalid under 35 U.S.C. 5 103 for obviousness. 

U.S. Patent No. 6,040,160 is unenforceable due to inequitable conduct. 

U.S. Patent No. 5,827,698 is unenforceable due to inequitable conduct. 

U.S. Patent No. 6,040,160 is not unenforceable due to unclean hands. 

U.S. Patent No. 5,827,698 is not unenforceable due to unclean hands. 

10. 

1 1. 

12. 

13. 

14. 

15. 

16. 

146 
INITIAL DETERMINATION 

Based on the foregoing opinion, findings of fact, conclusions of law, the evidence, and the 

record as a whole, and having considered all pleadings and arguments, including the proposed 

findings of fact and conclusions of law, it is the Administrative Law Judge’s Initial Determination 

that a violation of Section 337 of the Tariff Act of 1930, as amended, has not been found in the 

importation into the United States, the sale for importation, or the sale within the United States after 

importation of certain L-lysine feed products, their methods of production and genetic constructs for 

production. 

The Administrative Law Judge hereby CERTIFIES to the Commission this Initial 

Determination, together with the record of the hearing in this investigation consisting of the 

following: the transcript of the evidentiary hearing, with appropriate corrections as may hereafter be 

ordered by the Administrative Law Judge; and Mer the exhibits accepted into evidence in this 

investigation as listed in the attached exhibit lists. 

Pursuant to 19 C.F.R. 9 2 10.42(h), this Initial Determination shall become the determination 

of the Commission unless a party files a petition for review pursuant to 19 C.F.R. 5 21 0.43(a) or the 

Commission, pursuant to 19 C.F.R. 9 210.44, orders on its own motion a review of the Initial 

Determination or certain issues therein. 

147 
RECOMMENDED DETERMINATION ON REMEDY AND BOND 

Pursuant to Commission Rules 2 10.36(a) and 21 0.42(a)( l)(ii), the Administrative Law Judge 

is to consider evidence and argument on the issues of remedy and bonding and issue a recommended 

determination thereon. 

VIII. Remedy and Bonding 

A. Limited Exclusion Order 

Under Section 337(d), the Commission may issue either a limited or a general exclusion order. 

A limited exclusion order instructs the U.S. Customs Service to exclude from entry all articles that 

are covered by the patent at issue and that originate from a named respondent in the investigation. 

Ajinomoto requests that an exclusion order be issued that prohibits the importation of GBT’s 

infringing The Staff argues that if a violation is found a limited exclusion order should 

i~sue.7~’ The undersigned finds in this investigation that if a violation is found, the appropriate 

remedy would be a limited exclusion order directed to GBT’s old Escherichia coli bacteria strain 

deposited under Accession No. SD-5590. 

By stipulation, the parties have agreed that should an exclusion order issue that such an order 

include a certification provision. Specifically, the parties stipulate as follows: 

Pursuant to procedures to be specified by the Bureau of Customs and Border 

Protection (“Customs”), as Customs deems necessary, persons seeking to import Llysine feed products produced by Global Bio-Chem Technology Group Company 

Limited, Changchun Dacheng Bio-Chem Engineering Development Co., Ltd., 

Changchun Baocheng Bio-Chem Development Co., Ltd., Changchun Dahe Bio 

Technology Development Co., Ltd. or Bio Chem Technology (HK) Limited 

(collectively “GBT”) that are potentially subject to this Order may be required to 

certify that they are familiar with the terms of this Order, that they have made 

740 CRB at 35. 

741 SIB at 73. 

148 
appropriate inquiry, and thereupon state that, to the best of their knowledge and belief, 

the products being imported are not excluded from entry under paragraphs - through - 

of this Order, including because they were manufactured using the Corynebacterium 

strain deposited with the ATCC under Accession #SD-5620 or they were 

manufactured using the E. coli bacterium strain deposited with the ATCC under 

Accession #SD-57 1 7, it being understood that incidental contamination of the product 

does not constitute a violation of such certification. At its discretion, Customs may 

require persons who have provided the certification described in this paragraph to 

furnish such records or analysis as are necessary to substantiate the certification.742 

Based on the above stipulation, the undersigned recommends that any limited exclusion order that 

issues in this investigation include a certification provision as requested by the parties. 

B. Cease and Desist Order 

Under Section 337(f)( l), the Commission may issue a cease and desist order in addition to, 

or instead of, an exclusion order. Cease and desist orders are warranted primarily when the 

respondent maintains a commercially significant inventory of the accused products in the United 

States.743 Ajinomoto has not put forth any evidence that GBT maintains any inventory of lysine made 

by the accused method in the United States. In fact, Ajinomoto has not even briefed this issue in its 

post hearing briefs. Thus, there is no basis in the record to support the issuance of a cease and desist 

order in this investigation. Accordingly, the undersigned does not recommend a cease and desist 

order issue in this investigation. 

C. 

If the Commission enters an exclusion order or cease and desist order, parties may continue 

to import and sell their products during the pendency of the Presidential review under a bond in an 

amount determined by the Commission to be “sufficient to protect the Complainants fiom any 

Bond During Presidential Review Period 

742 JX-19OC at 7 14. 

743 Certain Crystalline, 15 U.S.P.Q.2d at 1277-79. 

149 
injury.”744 Ajinomoto does not brief this issue. The Staff asserts that the record does not contain any 

information that could serve as a basis for determining an appropriate bond and thus recommends that 

no bond be imposed on GBT during the presidential review period.745 GBT argues that if a bond is 

imposed, the amount of the bond should be minimal, but not to exceed 5% of the entered value of the 

imported goods.746 

In this case, Ajinomoto did not introduce any evidence of current sales or pricing information 

that would permit the undersigned to determine a price differential. Nor did Ajinomoto introduce 

evidence of a reasonable royalty rate. Thus, the undersigned has no basis in the record for 

determining an appropriate bond. In Certain Rubber Antidegradants, the Commission rejected a 

request for a 100% bond holding that “the complainant had the burden of supporting any proposition 

it advances, including the amount of the bond.”747 Because Ajinomoto has failed to provide any 

evidence that could be used as a basis for determining a bond amount and because Ajinomoto failed 

to address this issue in its post-hearing brief, the undersigned would recommend in this investigation 

that if a violation is found that no bond be required during the Presidential review period. 

Within seven days of the date of this document, each party shall submit to the office of the 

Administrative Law Judge a statement as to whether or not it seeks to have any portion of this 

document deleted from the public version. The parties’ submissions must be made by hard copy by 

the aforementioned date. 

Any party seeking to have any portion of this document deleted from the public version 

744 19 U.S.C. 0 1337(e); 19 C.F.R. 5 210.50(a)(3). 

745 SIB at 73. 

746 RIB at 78. 

747 Certain Rubber Antidegradants, Inv. No. 337-TA-533, Commission Opinion at 40 

(2006). 

150 
thereof must submit to this office a copy of this document with red brackets indicating any portion 

asserted to contain confidential business information. The parties’ submission concerning the public 

version of this document need not be filed with the Commission Secretary. 

SO ORDERED. 

Administrative Law Judge 

151 
APPENDIX OF EXHIBIT LISTS 

A1 
UNITED STATES INTERNATIONAL TRADE COMMISSION 

Washington, D.C. 

EXHIBIT DESCRIPTION/ TITLE 

NUMBER 

JX-001 US. Patent No. 6,040,160 

JX-002 U.S. Patent No. 5,827,698 

JX-003 

(AHL 000713-000766) 

(AHL OoooO1-oooO21) 

0511996 Transmittal Letter re US. 

Patent Application No. 081648,010 

JX-004 (‘160) Japanese Patent Application 

JX-005 US. Patent Application No. 

(AAHL 000466-000634) 

(AAHLOO 19 12-001940) 

08/849,212 for “Novel Lysine 

Decarboxylase Gene and Method of 

Producing L-Lysine” 

JX-006 (‘698) Japanese Patent Application 

JX-007C E.coli development plan 

(AAHL 000005-000155) 

(AAHL 000070-000102) 

(AHL 4293 18) 

Before The Honorable Charles E. Bullock 

PURPOSE 

Validity, 

enforceability 

Validity, 

enforceability 

Validity 

Validity 

Validity 

Validity 

Validity, 

enforceability 

I IN THE MATTER OF 

CERTAIN L-LYSINE FEED PRODUCTS, 

WITNESS 

Kawamura 

Kikuchi 

Stipulation of the 

Parties 

Kojima 

Stipulation of the 

Parties 

I Investigation No. 337-TA-57 1 THEIR METHODS OF PRODUCTION AND 

GENETIC CONSTRUCTS FOR 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

31 17/08 

I PRODUCTION 

Koj ima 

COMPLAINANTS’ FINAL LIST OF “RIAL EXHIBITS 

Complainants hereby submit the parties’ Joint Exhibit List and Complainant’s Final List 

of Trial Exhibits. 

3/17/08 

JOINT TRIAL EXHIBITS 

Kojima 3/17/08 

SPONSORING I ADMITTED 

OHS Wesr:2M1111067.2 1 
JX-0 1 OC 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Webb 

JJX-OLZC 

ADMITTED 

311 7/08 

3/17/08 

3/17/08 

1 JX-013C 

Lab Notebook (AHL 429190- 

429209) 

Monthly Research Reports for 

I JX-016C 

Validity, 

enforceability 

Validity, 

JX-0 17C tKojima 

JX-O 18C 

JX-0 19C 

JX-02OC 

JX-021C 

JX-022C 

JX-023C 

JX-024C 

31 17/08 

DESCRIPTION/ TIT= I PURPOSE 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Kawamura 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Lab Notebook (AHL 429210- 

4293 19) 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

- 3/17/08 

3/ 17/08 

3/17/08 

- 

31 17/08 

- 3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

Validity, 

enforceability 

11/1990 (AHL 430879-430881) 

Monthly Research Reports for 

10/1990 (AHL 430882-430884) 

Monthly Research Reports for 

121990 (AHL 430876-78 ) 

Monthly Research Reports for 

021991 (AHL 430870-430872) 

Monthly Research Reports for 

0811991 (AHL 430846430847) 

Monthly Research Reports for 

01/1992 (AHL 430820-430823 ) 

Monthly Research Reports for 

02/1992 ( AHL 430816-430818 ) ~ 

2nd Lysine Project Research Report 

No. 11370 

Monthly Research Reports for 

0811990 (AHL 430844-430845 ) 

(AHL 002992-003014) 

~ 

Monthly Research Reports for 

0911990 (AHL 430838-30839) 

Monthly Research Reports for 

Monthly Research Reports for 

0911993 (A€% 430757-430758 ) 

Monthly Research Reports for 

Monthly Research Reports for 

Monthly Research Reports for 

0311992 (AHL 430811-430813) 

OW991 (AHL 430873-430875 ) 

Dl11994 (AHL 430725-430730) 

33/1991 (AHL 430867-430869) 

enforceability 

enforceability 

, enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

OHS West:260411067.2 2 
EXHIBIT 

NUMBER 

JX-025C 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

JX-026C 

JX-027C 3/17/08 

3/17/08 

+ 

JX-028C 

Validity, 

enforceability 

K-029C 

JX-03OC 

Stipulation of the 3/17/08 

Parties 

JX-03 1C 

JX-032c 

I 

Validity, Koj ima 

enforceability 

JX-033C 

3/17/08 

JX-034C 

IX-035C 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

IX-036C 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

IX-037C 

IX-038C , 

IX-039C 

'X-04 1 C 

DESCXIPTION/ TITLE 

Monthly Research Reports for 

0411991 (AHL 430860-430862 ) 

Monthly Research Reports for 

0611991 (AHL 430853-430855 ) 

Monthly Research Reports for 

07/1991 (AHL 430849-430852) 

Monthly Research Reports for 

02/1994 (AHL 430718-21 & 

430723-24 ) 

Monthly Research Reports for 

1011991 (AHL 430833-430836) 

Monthly Research Reports for 

12/1991 (AHL 430824-430827 ) 

Monthly Research Reports for 

03/1994 (AHL 430712-430717) - 

Monthly Research Reports for 

04/1994 (AHL 430706-4307 1 1) 

Monthly Research Reports for 

05/1994 (AHL 430700-430705) 

Monthly Research Reports for 

08/1995 (AHL 430608 & 430613) 

Monthly Research Reports for 

07/1994 (AHL 430688-430693) 

Monthly Research Reports for 

OW1994 (AHL 430682-430687) 

3rd Lysine Project Research Report 

No. 11416 

(AHL 003015-003050) 

Monthly Research Reports for 

04/1993 (AHL 430779-430782) 

Monthly Research Reports for 

D5/1993 (AHL 430775-430778) 

Monthly Research Reports for 

36/1993 (AHL 430771-430774) 

Monthly Research Reports for 

07/1993 (AHL 430765-430770) 

PURPOSE I SPONSORING I ADMITTED 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Parties 

Kikuchi 3/17/08 

3/17/08 

3/ 17/08 

31 17/08 

3/ 1 7/08 

3/ 17/08 

Validity, Kojima 3/17/08 

enforceability 

Validity, Kawamura 3/17/08 

enforceability 

Validity, 3/17/08 

enforceability 

Validity, Kawamura 3/17/08 

enforceability t Validity, Kawamura 3/17/08 

znforceabi 1 it y 

OHS West:26W11067.2 3 
' EXHIBIT DESCRIPTION/ TITLE PURPOSE 

NUMBER 

JX-042C Monthly Research Reports for Validity, 

JX-043C Monthly Research Reports for Validity, 

JX-044C Monthly Research Reports for Validity, 

0811993 (AHL 430759-430764) enforceability 

0911994 (AHL 430676-430681) enforceability 

10/1993 (AHL 430746-430751) enforceability 

No. 11815 enforceability 

(AHL 003084-3 102) 

1011994 (AHL 430670-430675 ) enforceability 

11/1994 (Am 430663-430669) enforceability 

1211994 (AHL 430657-430662) enforceability 

JX-045C 6th Lysine Project Research Report Validity, 

JX-046C Monthly Research Reports for Validity, 

JX-047C Monthly Research Reports for Validity, 

JX-048C Monthly Research Reports for Validity, 

JX-049C Monthly Research Reports for Validity, 

JX-051C 

JX-052C 

JX-053C 

JX-054C 

JX-055C 

JX-056C 

SPONSORING ADMITTED 

WITNESS 

Stipulation of the 3/17/08 

Parties 

Stipulation of the 3/17/08 

Parties 

Stipulation of the 3/17/08 

Parties 

Webb 31 17/08 

Stipulation of the 3/17/08 

Parties 

Stipulation of the 31 17/08 

Parties 

Stipulation of the 3/17/08 

Paaies 

Stipulation of the 3/17/08 

OU1995 (AHL 430645-430649) 

Monthly Research Reports for 

0311995 (AHL 430638-430644) 

10th Lysine Project Research 

Report No. 11819 

7th Lysine Project Research Report 

No. 11816 

13th Lysine Project Research 

Report No. 1 1901 

Monthly Research Reports for 

09/199 1 (AHL 430840-43084 1) 

1st Lysine Project Research Report 

No. 11369 

Monthly Research Reports for 

0911995 (Am 430607-43061 1) 

(AHL 003171-003187) 

(AHL 003103-3131) 

(AHL 003156-3170) 

(AHL 435942-435969) 

OHS West:260411067.2 

enforc&bility Pkes 

Validity, Kikuchi 3/17/08 

enforceability 

Validity, Kikuchi 3/17/08 

enforceability 

Validity, Webb 3/17/08 

enforceability 

Validity, Stipulation of the 3/17/08 

enforceability Parties 

Validity, Stipulation of the 3/17/08 

enforceability Parties 

Validity, Koj ima 3/17/08 

enforceability 

Validity, Nakiiiski 3/17/08 

enforceability 

4 
EXHIBIT 

NUMBER 

JX-057C 

JX-058C 

JX-059C 

JX-06OC 

JX-061C 

JX-062C 

JX-063C 

rx-064C 

rx-065C 

1x466 

IX-067C 

'X-068C 

X-069C 

X-07OC 

X-07 1 

X-072 

X-073C 

OHS West:260411067.2 5 

DESCRIPTION/ TITLE PURPOSE SPONSORING ADMlTTED 

Nishimura Monthly Reports Validity, Stipulation of the 3/17/08 

(AHL 436344-436360) enforceability Parties 

Junichiro Kojima Monthly Reports Validity, Stipulation of the 31 17/08 

(AHL 436361-436382) enforceability Parties 

Nakanishi Monthly Reports Validity, Stipulation of the 3/17/08 

(AHL 437016-437048) enforceability Parties 

Monthly Research Reports for Validity, Webb 3/17/08 

1211993 (AHL 430731-430737 ) enforceability 

Monthly Research Reports for Validity, Stipulation of the 3/17/08 

01/1992 (AJB-430819) enforceability Parties 

Monthly Research Reports for Validity, Stipulation of the 3/17/08 

05/1991 (AHL 430856-430859) enforceability Parties 

Monthly Research Reports for Validity, Stipulation of the 3/17/08 

OW1991 (AHL 430863) enforceability Parties 

Monthly Research Reports for Validity, Stipulation of the 3/17/08 

131990 (AHL 430864-65) enforceability Parties 

Monthly Research Reports for Validity, Stipulation of the 3/17/08 

loll990 and 1111990 enforceability Parties 

(AHL430866) 

Withdrawn 

Withdrawn 

Withdrawn 

Monthly Research Reports for Validity, Stipulation of the 311 7/08 

10/1995 (AHL 430601-606) enforceability Parties 

Compilation of experimental result Validity, Stipulation of the 3/17/08 

charts enforceability Parties 

(AHL 430404-430473) 

11/06/1997 Deposit record for strain Validity, Stipulation of the 3/17/08 

WC196 enforceability Parties 

(AHL 500000) 

AJ13069 with a public depository enforceability 

(AHL 434302-4343 13) 

15th Lysine Project Research Validity, Kikuchi 3/17/08 

Report No. 12230 enforceability 

WITNESS 

Request to make a deposit of strain Validity, &chi 3/17/08 

(AHL 003 188-3207) 
EXHIBIT 

NUMBER 

JX-074C 

JX-075c 

JX-076C 

JX-077C 

JX-078C 

JX-079c 

JX-080C 

JX-081C 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Kikuchi 

Stipulation of the 

Parties 

Kawamura 

Kawamura 

Kawamura 

JX-082C 

IX-083C 

JX-084C 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

JX-ossc 3/17/08 

JX-086C 

JX-087C 

IX-088C 

IX-089C 

IX-09OC 

Webb 

DESCRIPTION/ TITLE 

3/17/08 

Monthly Research Reports for 

Monthly Research Reports for 

0511995 (AHL 430628-430633 ) 

0411995 (AHL 430634-430637) 

Webb 

Webb 

-~ 

Monthly Research Reports for 

0611995 (AHL 430623-430627 ) 

3/17/08 

3/17/08 

~ 

Monthly Research Reports for 

0711995 (AI-E 430617-430622 ) 

Monthly Research Reports for 

1111995 (AHLA305961430600 ) 

Monthly Research Reports for 

12/1995 (a 430590-430595) 

Monthly Research Reports for 

11/1991 (AHL 430829-430832) 

14th Lysine Project Research 

Report No. 11902 

Monthly Research Reports for 

0411992 (AHL 430806-430808) 

Monthly Research Reports for 

0511992 (AHL 430803-430805) 

(AHL 433696-433742) 

Monthly Research Reports for 

Monthly Research Reports for 

Monthly Research Reports for 

06/1992 (AHL 430800-430802) 

0711992 (AHL 430798-430799) 

08/1992 (AHL 430796-430797) 

Monthly Research Reports for 

3911992 (AHL 430794-430795) 

Withdrawn 

Monthly Research Reports for 

10/1992 (A€% 430793 & 430522) 

VIonthly Research Reports for 

1111992 (AHL 430791-430792) 

PURPOSE 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

SPONSORING I ADMITTED 

wsbb 3/17/08 

OHS West:260411067.2 6 
EXHIBIT 

NUMBER 

JX-091C 

JX-092C 

JX-093C 

JX-094C 

JX-095C 

JX-096C 

JX-097C 

JX-098C 

JX-099C 

JX-looC 

Jx-101 

JX-102 

rx-io3 

DESCRIPTION/ TITLE 

Monthly Research Reports for 

12/1992 (AM, 430789-430790) 

Monthly Research Reports for 

01/1993 (AHL 430787430788) 

Monthly Research Reports for 

02/1993 (AHL, 430785-430786) 

Monthly Research Report for 

03/1993 (AHL 430783-430784) 

5th Lysine Project Research Report 

No. 11530 

9th Lysine Project Research Report 

No. 11818 

(AKL 003051 -003082) 

(AHL 436040-436057) 

Withdrawn 

1 lth Lysine Project Research 

Report No. 11820 

(Am 43 605 8 -436095) 

Withdrawn 

Withdrawn 

Alvarez-Jacobs, J. et al., “Lysine 

and Methionine Overproduction by 

an Escherichia coli Strain 

Transformed with Pseudomonas 

acidovorans DNA,” Biotechnology 

Letters 12:425-430 (1990) 

Applebaum, D. M. et al., 

“Comparison of the Biosynthetic 

and Biodegradative Ornithine 

Decarboxylases of Escherichia 

20li,” Biochem. 16:1580-1584 

c1977) 

Bouvier, J. et al., “Nucleotide 

Sequence and Expression of the 

Sscherichia coli dapB Gene,” J. 

3iol. Chem. 259:14829-14834 

:1984) 

PURPOSE 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Background, 

validity 

Background, 

validity 

Background, 

validity 

SPONSORING 

WITNESS 

Kawamura 

Kawamura 

Koj ima 

Kawamura 

Kawamura 

Kawamura 

Kojima 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

ADMITTED 

3/17/08 

3/17/08 

3/17/08 

311 7/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

OHS West:26041 1067.2 7 
EXHIBIT 

NUMBER 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

JX-104 

3/ 17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

JX-105 

JX- 106C 

Stipulation of the 

Parties 

~ 

JX- 107C 

JX- 108 

3/17/08 

JX- 109C 

JX-1 1OC 

JX-111C 

rx-112 

DESCRIPTION/ TJTLE 

Bukhari, AI. and Taylor, AL., 

“Genetic Analysis of 

Diaminopimelic Acid- and LysineRequiring Mutants of Escherichia 

coli,” J. Bacteriol. 105:844-54 

(1971) 

Busby, S. M. et al., “Isolation of 

mutant promoters on the 

Escherichia coli galactose operon 

using local mutagenesis on cloned 

DNA fragments,” J. Mol. Biol. 

154: 197 (1982) 

Employment invention reporting 

form for “A Novel Lysine 

Decarboxylase Gene” (AHL 

434373) 

05/06/1997 Employment invention 

reporting form re Japan as being the 

designated state for a PCT filing 

Prosecution file history for ‘698 

patent (AAHL00000 1-463) 

(AHL 434374) 

11/26/1993 Employment invention 

reporting form corresponding to the 

patent application that is Exh. 4 

(AHL 434375) 

Employment invention reporting 

form for the Japanese national phase 

Df WIPO Publication of PCT 

Application No. PcT/JP94/0 1994 as 

WO 95116042, (Foreign Counterpart 

3f ‘160 patent) (AHL 434376) 

16th Lysine Project Research 

Xeport No. 12231 

:AHL 436128-436143) 

?rosecution file history for the ‘160 

latent (AAHLOOO464-204 1) 

PURPOSE 

Background, 

validity 

Background, 

validity 

Validity, 

background, 

enforceability 

Validity, 

background, 

enforceability 

Validity, 

background, 

enforceability 

Validity, 

background, 

enforceability 

Validity, 

background, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

SPONSORING I ADMITTED 

Parties 

Stipulation of the 3/17/08 

Parties 

I 

the I 3/17/08 

OHS Wac2604 I 1067.2 8 
EXHIBl 

NUMBE 

JX- 113 

JX- 1 14 

JX-115 

JX- 1 16 

IX-117 

IX-118 

’X-119 

DESCRIPTION/ TITLE 

Deposit Receipt of a microorganism 

with translation (OSMMN000141- 

142) 

Deposit Receipt of a microorganism 

with translation (OSMMN000143- 

144) 

Canellakis, E. S. et ai., “Regulation 

of polyamine biosynthesis by 

antizyme and some recent 

developments relating the induction 

of polyamine biosynthesis to cell 

growth,” Bioscience Reports 5:189- 

204 (1985) 

Cassan, M. et al., “Nucleotide 

Sequence of lysC Gene Encoding 

the Lysine-Sensitive Aspartokinase 

[I1 of Escherichia coli K 12: 

Evolutionary Pathway Leading to 

kee Isofunctional Enzymes,” J. 

Biol. Chem. 261:1052-1057 (1986) 

3an0, K., and Shiio, I., “Microbial 

%duction of L-Lysine: UU. 

bduction by Mutants Resistant to 

5 -(2Aminoethyl)-L-C y steine,” J. 

Sen. Appl. Microbiol. 16:373-391 

1970) 

3rock. R. D. et al., “The 

nodification of the amino acid 

:omposition of higher plants by 

nutation and selection,” Caplus 

lccess No: 174:488102 Caplus 

1973) 

littel, et al., “Characterization of a 

.ysine-insensitive Form of 

Iihydrodipicolinate Synthase from 

4aize.” In Biosynthesis and 

dolecular Regulation of Amino 

Acids in Plants, BK Singh, H.E. 

lores and J.C. Shannon, eds. 

unerican Society of Plant 

PURPOSE 

Validity, 

enforceability 

Validity, 

enforceability 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Webb 

Webb 

ADMITTED 

3/17/08 

3/ 17/08 

311 7/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

I 

OHS Wat:2604110672 9 
EXHLBIT 

NUMBER 

JX- 120 

JX- 12 1 C 

JX- 122 

JX- 123 

JX- 124 

JX- 125 

rx- 126 

r X- 127C 

DESCRIPTION/ TITLE 

Hermann, M. et al., “Consequences 

of Lysine Oversynthesis in 

Pseudomonas Mutants Insensitive to 

Feedback Inhibition,” Eur. J. 

B iochem. 30: 100- 106 ( 1 972) 

Monthly Research Reports for 

1111993 (AHL 43074430745) 

Chan, E-C, “Disruption of targeted 

gene in bacterial chromosome by 

using a temperature-sensitive 

plasmid,” Biochem. Biophys. Res. 

Comm. 194525 530 (1993) 

Reverend, B. D. et al., 

“Improvement of Escherichia coli 

Strains Overproducing Lysine Using 

Recombinant DNA Techniques,” 

Eur. J. Appl. Microbiol. 15:227-231 

(1982) 

Tabor, H., Hafner, E. W., and 

Tabor, C. W., “Construction of an 

Escherichia coli Strain Unable to 

Synthesize Putrescine, Spermidine, 

or Cadaverine: Characterization of 

Two Genes Controlling Lysine 

Decarboxylase,” J. Bacteriol. 

Wertheimer, S. J., and Leifer, Z., 

“Putrescine and Spermidine 

Sensitivity of Lysine Decarboxylase 

in Escherichia coli: Evidence for a 

Constitutive Enzyme and its Mode 

of Regulation,” Biochem. Biophys. 

Res. Comm. 114:882 888 (1983) 

Soldemberg, S., “Lysine 

Decarboxylase Mutants of 

Escherichia coli: Evidence for Two 

Enzyme Forms,” J. Bacteriol. 

tth Research Report No. 11529 

AHL 435970-435993) 

1441952-956 (1980) 

141: 1428- 143 1 (1980) 

PURPOSE 

Background, 

validity 

Validity, 

enforceability 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Eiackground, 

ralidity 

Jalidity, 

sforceability 

SPONSORING 

WITNESS 

Webb 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Somerville 

Kawamura 

ADMITTED 

3 / 17 /OS 

3/ 17108- 

3/17/08- 

3/17/08 

311 7/08 

3/17/08 

3/17/08 

3117108- 

OHS West26041 1067.2 10 
EXHIBIT 

NUMBER 

JX-128C 

JX-129C 

JX- 130 

JX-13lC 

JX-132 

JX- 1 33 

IX- 134 

IX-135 

DESCRIPTION/ TITLE PURPOSE SPONSORING ADMITTED 

12th Research Report No. 11900 Validity, Stipulation of the 

(AHL 003 132-003 155) enforceability Parties 

17th Research Report No. 12232 Validity, Stipulation of the 

(AHL 43 3743 -433774) enforceability Parties 

Moms, D. R. and Boeker, E. A, Stipulation of the 

“Biosynthetic and Biodegradative validity Parties 

Ornithine and Arginine 

Decarboxylases from Escherichia 

coli,” Methods in Enzymol. 94:125- 

134 (1983) 

20th Research Report No. 12468 Validity, Stipulation of the 

(AHL 003233-003271) enforceability Parties 

Igarashi, K. et al., “Formation of a Background, Webb 

Compensatory Polyamine by validity 

Escherichia coli PolyamineRequiring Mutants during Growth 

in the Absence of Polyamines,” 1. 

Bacteriol. 166: 128-134 (1986) 

Ravnikar, P. D., Somerville, R. L, Background, Stipulation of the 

“Localization of the structural gene validity Parties 

for threonine dehydrogenase in 

Escherichia coli, “ J. Bacteriol. 

16$:434-436 (1986) 

Cohen, S. A et al.. “Construction of 

biologically functional bacterial validity Parties 

plasmids in vitro,” Proc. Natl. Acad. 

Sci. 70:3240-3244 (1973) 

Cunningham-Rundles, S., and Maas, Background, Stipulation of the 

W. K., “Isolation, Characterization, validity Parties 

and Mapping of Escherichia coli 

Mutants Blocked in the Synthesis of 

Ornithine Decarboxylase,” J. 

Bacteriol. 124:791-799 (1975) 

WITNESS 

Background, 

Background, Stipulation of the 

3/17/08 

31 17/08 

3/17/08 

3/ 17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

OHS West:2M)4 11067.2 11 
EXHIBIT 

NUMBER 

JX-136 

JX-137 

JX-138 

IX-139 

IX- 140 

’X-141 

Background, 

validity 

X- 142 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

DESCRIPTION/ TITLE ADMITTED 

Dobson et al., 3/17/08 ‘The crystal 

structures of native and (S)-lysinebound dihydrodipicolinate synthase 

from Escherichia coli with 

improved resolution show new 

features of biological significance,” 

Acta Cryst. D61:1116-1124 (2005) 

(GBT217852-217860) 

Farmer, J.J. ITI et al., “Biochemical 

identification of new species and 

biogroups of Enterobacteriaceae 

isolated from clinical specimens,” J. 

of Clin. Microbiol., 21:46-76 (1985) 

Fecker, L. F. et al., “Cloning and 

characterization of a lysine 

decarboxylase gene from Hafni 

alvie,” Molecular Genetics and 

Genomics 203~177-184 (1986) 

Hamilton, C. M. et al., “New 

Method for generating deletions and 

gene replacements in Escherichia 

coli,” J. Bacteriol. 171:4617-4622 

(1989) 

Ingram, V. M., “Gene Mutations in 

Human Hemoglobin. The Chemical 

Difference Between Normal and 

Sickle Cell Hemoglobin,” Nature 

Jacob, F., and Monod, J., “Generic 

Regulatory Mechanisms in the 

Synthesis of Proteins,” I. Mol. Biol. 

180~326-328 (1957) 

3:3 18-356 (1961) 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

?arties 

lasin, M., Schimmel, P., “Deletion 

3f an essential gene in Escherichia 

:oli by site-specific recombination 

Nith linear DNA fragments,” J. 

3acteriol. 159:783-786 (1984) 

3/17/08 

3/17/08 

3/17/08 

PURPOSE 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

lralidity 

3ackg~ound, 

validity 

Parties 

Parties 

OHS West:260411067.2 12 
EXHIBIT 

NUMBER 

/PURPOSE 

JX-143 Background, 

~ validity 

JXTl44 

JX- 145 

JX-146 

JX- 147 

Background, 

l validity 

JX- 148 

JX- 149 

IX- 150 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

DESCRIPTION/ TITLE ADMITTED 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

Kadonaga, J. T., and Knowles, J. R.. 

“A simple and efficient method for 

chemical mutagenesis of DNA,” 

Nucleic Acids Res. 13:1733 (1985) 

Kamio, Y., and Terawaki, Y ., “Purification and Properties of 

Selenomonas reminantium Lysine 

Decarboxylase,” J. Bacteriol. 

Kironde, F. A et al., “Random 

mutagenesis of the gene for the 

beta-subunit of F1-ATPase from 

Escherichia coli,” Biochem. J. 

259:421426 (1989) 

Kohara, Y. et al., ‘The physical map 

of the whole E. coli chromosome: 

Application of a new strategy for 

rapid analysis and sorting of a large 

genomic library,” Cell 50:495-508 

Koonin, E. et al., “Sequencing and 

Analysis of Bacterial Genomes,” 

Current Biology 6:4O4-4 16 (1 996) 

153~658-664 (1983) 

Li, S., and Cronan, J. E., “The 

Genes Encoding the Two 

Carboxyltransferase Subunits of 

Escherichia coli Acetyl-coA 

Carboxylase,” J. Biol. Chem. 

Lidholm, J., and Gustafsson, P., 

“Homologues of the green algal 

gidA gene and the liverwort frxC 

gene are present on the chloroplast 

genomes of conifers,” Plant Mol. 

Biol. 17:787-798 (1991) 

Lobban, P., and Kaiser, A D., 

,‘Enzymatic end-to-end joining of 

DNA molecules,” J. Mol. Biol. 

79:453-471(1973) 

267: 16841- 16847 (1992) 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Stipulation of the I 31 17/08 

OHS West:260411067.2 13 
JX-157 

JX-158 

DESCRIIYTIONI TITLE 

Matsushime, L. H. et al., “Human cros-1 gene homologues to the v-ros 

sequence of UR2 sarcoma virus 

encodes for a transmembrane 

receptorlike molecule,” Mol. Cell 

Biol. 6:3000-3004 (1986) 

Matsuyama. S., and Mizushima, S., 

“Construction and characterization 

of a deletion mutant lacking micF, a 

proposed regulatory gene for OmpF 

synthesis in Escherichia coli,” J. 

Bacteriol. 162:1196-1202 (1985) 

Mertz, J. E. et al., “Cleavage of 

DNA by RI restriction 

endonucleases generates cohesive 

ends,” Roc. Natl. Acad. Sci. 

Mirwdtd, C. et al., ‘The Crystal 

Structure of Dihydrodipicolinate 

Synthase from Escherichia coli at 

2.5 A Resolution,” J. Mol. Biol. 

69~3370-3374 (1972) 

246:227-239 (1995) ~ 

Yumber intentionally not used 

?atte, J. C. et al., “Regulation of 

Lysine Biosynthesis in Escherichia 

:oli K12*,” Acta Microbiol. Acad. 

ici. Hung. 23:121-128 (1976) 

’atte, J. C. et al., “Role of the 

,ysine-Sensitive Aspartokinase II in 

he Regulation of DAPIecarboxylase Synthesis in 

3cherichia coli K12.” FEBS 

stters 43:67-70 (1974) ~ 

’opkin, P. S., and Mass, W., 

Escherichia coli Regulatory 

dutation Affecting Lysine 

’ransport and Lysine 

Iecarboxylase,” J. Bacteriol., 

41:485-492 (1980) 

PURPOSE 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

B ackgound, 

lralidity 

3ackgound, 

ralidity 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

~~ 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

ADMTTTED 

~ 

3/17/08 

31 17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

OHS West:260411067.2 14 
EXHIBIT 

NUMBER 

JX- 159 

WITNESS 

Stipulation of the 

Parties 

JX- 160 

JX-161 

31 17/08 

JX- 162 

JX- 163 

JX-164 

JX- 165 

JX- 166 

Stipulation of the 

Parties 

__~~ 

DESCRIPTION/ TITLE 

3/17/08 

Prober, J. M. et al., “A System for 

Rapid DNA Sequencing with 

Fluorescent Chain-Terminating 

Dideoxynucleotides,” Science, 

Ren, S-X et al., “Unique 

physiological and pathogenic 

features of Leptospira interrogans 

revealed by whole-genome 

sequencing,” Nature 422,888-493 

(2003) 

238:336-341 (1987) 

Stipulation of the 

Parties 

Richaud, F. et al., “Chromosomal 

Location and Nucleotide Sequence 

of the Escherichia coli dapA gene,” 

J. Bacteriol. 166:297-300 (1986) 

Roberts, R. J., “Restriction enzymes 

and their isoschizomers,” Nucleic 

Acid Res. 16 suppl:r271313 (1988) 

Roberts, R. J., “Restriction and 

modification enzymes and their 

recognition sequences,” Nucleic 

Acid Res. ll:r135-r167 (1983) 

Rood, J. I. et. al, “Characterization 

of Monofunctional Chorismate 

MutasePrephenate Dehydrogenase 

Enzymes Obtained via Mutagenesis 

of Recombinant Plasmids in vitro,” 

Eur. J. Biochen 124: 513-519 

(1982) 

3/17/08 

~ 

Sahm, H., “Metabolic Design in 

Amino Acid-Producing Bacteria,” 

Institut fir Biotechnologie, pp. 55- 

62 (1990) 

Saiki, R. K. et al., ‘Primer-directed 

enzymatic amplification of DNA 

with a thermostable DNA 

polymerase,” Science 239:487 

(1988) 

Stipulation of the 

Parties 

PURPOSE 

311 7/08 

Background, 

validity 

Stipulation of the 

Parties 

Background, 

validity 

3/ 17/08 

Background, 

validity 

Stipulation of the 

Parties 

Background, 

validity 

3/17/08 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

SPONSORING I ADMITTED 

Webb I 3/17/08 

Parties 

OHS Wat:26WI 1067.2 15 
JX- 167 

I 

JX- 168 

JX- 169 

JX- 170 

JX-171 

JX-172 

JX-173 

DESCRLPTIONI TITLE 

Sambrook, 1. et al.. “Molecular 

Cloning,” Cold Spring Harbor 

Laboratory, Sections 5.3-532,562- 

5.67, 11, 17:lO-17.16 (2nd ed. 

1989) 

Shaver, J. M. et al., “Single-amino 

acid substitutions eliminate lysine. 

inhibition of maize 

dihydrodipicolinate synthase,” Prw. 

Natl. Acad. Sci. 93:1962-1966 

(1996) 

Shortle, D., and Nathans, D., “Local 

Mutagenesis: A method for 

generating viral mutants with bases 

substitutions in preselected regions 

of the viral genome,*’ Proc. Natl. 

Acad. Sci. 7591702174 (1978) 

Singleton, C.K. et al., “DNA 

sequence of the E. coli trpR gene 

and prediction of the amino acid 

sequence of Trp repressor,” Nucl. 

Acids Res. 8: 1551-1560 (1980). 

Southern, E. M., “Detection of 

Specific Sequences Among DNA 

Fragments Separated by Gel 

Electrophoresis,” J. Mol. Biol., 

rsunekawa, H. et al., Acquisition of 

3 Sucrose Utilization System in 

Sscherichia coli K-12 Derivative 

md Its Application to Industry, 

4pplied and Environmental 

bficrobiology 58(6):208 1-2088 

‘1992) 

Jik, S. B. et al., “Mutagenesis of 

he a Subunit of the FlFO-ATPase 

rom Escherichia coli,” J. Biol. 

Xem. 263:6599-6605 (1988) 

98503-517 (1975) 

PURPOSE 

Background, 

Val idit y 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

ADMITTED 

3/17/08 

3/17/08 

31 17/08 

3/17/08 

3/17/08 

3/17/08 

3/17/08 

OHS Wesc26O4 I 1067.2 16 
EXHIBIT 

NUMBER 

JX- 1 74 

JX- 175 

JX-176 

JX- 177 

JX-178C 

JX- 179 

JX-180 

JX-181C 

DESCRIPTION/ TITLE 

Wahl, G. M. et al., “Molecular 

Hybridization of Immobilized 

Nucleic Acids: Theoretical 

Concepts and Practical 

Considerations,” Methods in 

En~ym01. 152~399-407 (1987) 

Weiss, B. A et al., “Enzymatic 

breakage and joining of 

deoxyribonucleic acid. VI. Further 

purification and properties of 

polynucoleotide ligase from 

Escherichia coli infected with 

bacteriophage T4,” J. Biol. Chem. 

243:4543 (1968) 

Yamamoto, Y. et d. ‘The 

Escherichia coli ldcC gene encodes 

another lysine decarboxylase, 

probably a constitutive enzyme.’ 

Genes Genet. Syst. 72: 167-172 

(1997). 

Yang, W. et al., “A stationary phase 

protein of Escherichia coli that 

affects the mode of association 

between the Trp repressor protein 

and operator-bearing DNA,” Proc. 

Natl. Acad. Sci. 905796 (1993) 

8th Lysine Project Research Report 

No. 11817 

Yugari, Y., and Gilvarg, C., 

“Coordinated end-product inhibition 

in lysine synthesis in Escherichia 

coli.,” Biochim. Biophys. Acta 

52:612414 (1962) 

Zoller, M. J., and Smith, M., 

‘Oligonucleotide-directed 

mutagenesis of DNA fragments 

:loned into M13 vectors,” Methods 

Withdrawn 

(AHL 435994-436039) 

EIU~~O~. 100:468-500 (1983) 

PURPOSE 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Background, 

validity 

Validity, 

enforceability 

Background, 

validity 

Background, 

validity 

SPONSORING 

w?TNEss 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Webb . 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

ADMITTED 

3/17/08 

31 17/08 

3/17/08 

3/17/08 

3f 17/08 

3/17/08 

3/17/08 

OHS West:26WI 1067.2 17 
JX- 184C 

JX-185 

Withdrawn 

Withdrawn 

Monthly Research Reports for 

OW993 (AHL 437296) rx-196c I 

JX-186C 

JX-187 

PURPOSE 

Withdrawn 

Meng, S., and Bennett, G., 

“Nucleotide Sequence of the 

Background, 

validity 

Webb 

Stipulation of the 

Parties 

Validity, 

enforceability 

3/17/08 

3/17/08 

Background Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Background 

3/17/08 

3/17/08 

3/10/08 

311 9/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

Unclean Hands 

Defense 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability ~~ 

Validity, 

dorceability 

Validity, 

mforceability 

WITNESS 

OHS West:26WI 1067.2 18 
EXHIBIT 

NUMBER 

JX- 199C 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

Kojima 

JX-2OOC 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

3/19/08 

31 19/08 

3/ 19/08 

3/19/08 

3/19/08 

JX-201 C 

EXHIBIT DESCRIPTION/ TITLE PURPOSE 

NUMBER 

JX-202C 

JX-203C 

JX-204C 

SPONSORING ADMTTED 

WITNESS 

JX-205C 

JX-206C 

JX-207C 

JX-208C 

JX-209C 

cx-001 I Number intentionally not used 

JX-21OC 

cx-002 

CX-003 

CX-004 

DESCRIPTION/ TITLE 1 PURPOSE I SPONSORING I ADMITTED 

Withdrawn 

Number intentionally not used 

Number intentionally not used 

Monthly Research Reports for 

1111993 (AHL 437299) 

Monthly Research Reports for 

1 111 993 (AHL 437300) 

Monthly Research Reports for 

12/1993 (AHL 437301) 

Monthly Research Reports for 

1211993 (AHL 437302) 

Monthly Research Reports for 

0111994 (AHL 437303) 

Monthly Research Reports for 

Monthly Research Reports for 

02/1994 (AHL 437305) 

Monthly Research Reports for 

02/1994 (AHL 437306) 

Monthly Research Reports for 

0311994 (AHL 437307) 

01/1994 (AHL 437304) 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Monthly Research Reports for 

0311994 (AHL 437308) 1 ~~$~bili~ 

Monthly Research Reports for 

D9/1993 (AHL 430752) 

Monthly Research Reports for 

35/1991 (AHL 430859) 

~ 

Validity, 

enforceability 

I 3/19/08 

Stipulation of the 

enforceability Parties 

Validity, I 

OHS Wst:2604110672 19 
. 

DESCRIPTION/ TITLE PURPOSE SPONSORING 

WITNESS 

EXHIBIT 

NUMBER 

ADMITTED 

CX-005 

CX-006C Withdrawn 

Withdrawn 

Withdrawn 

Global Bio-Chem Discussion 

Materials, January 2006 

(GBT105234- 105260) 

cx-007c 

Background, Motion by 3/19/08 

validity Complainants 

cx-008C 

cx-009c 

cx-010 

cx-011 

cx-0 12c 

CX-0 1 3 

CX-014 

CX-0 15 

CX-0 16C 

cx-017c 

CX-018C 

zx-0 19c 

cIx-02oc 

2X-021C 

"-022c 

ZX-023C 

2X-024C 

3X-025C 

2X-026C 

3X-027C 

ZX-028C 

IXO29C 

:X-O30C 

:X-03 1 C 

1X-032C 

I I I 

Number intentionally not used 

Number intentionally not used 

Withdrawn 

Withdrawn 

Number intentionally not used 

Number intentionally not used 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

flithdrawn 

Nithdrawn 

Withdrawn 

Withdrawn 

Nithdrawn 

Withdrawn 

Nithdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Yithdrawn 

Yithdrawn 

OHS West26041 1067.2 20 
EXHIBIT DESCFUPTION/ TITLE 

NUMBER 

CX-033C Withdrawn 

cX-034C Withdrawn 

CX-035 GBT promotional document 

CX-036 GBT promotional presentation 

CX-037 Number intentionally not used 

CX-038 Number intentionally not used 

CX-039 Number intentionally not used 

CX-040 Number intentionally not used 

CX-041 Number intentionally not used 

CX-042 Withdrawn 

CX-043 Number intentionally not used 

cx-044 Withdrawn 

CX-045 Number intentionally not used 

ZX-046 Number intentionally not used 

ZX-047 Number intentionally not used 

2X-048 Number intentionally not used 

2X-049C Bacterial Gene Reconstruction 

JX-050 Number intentionally not used 

3X-05 1 Number intentionally not used 

(GBT 109036- 109040) 

(GBT 119525-119545) 

Contract (GBT2133 15-3 17) 

I I I I 

3X-052C 1 Withdrawn 

PURPOSE SPONSORING ADMITTED 

WITNESS 

Background, Motion by 31 19/08 

validity Complainants 

Background, Motion by 3/19/08 

validity Complainants 

Background, Stipulation of the 311 9/08 

validity Parties 

JX-053 

3X-054 

1X-055 

3X-056 

1X-057 

Number intentionally not used 

Number intentionally not used 

Withdrawn 

Withdrawn 

Withdrawn 

OHS West:260411067.2 

1X-058 

:X-059 

21 

Withdrawn 

Withdrawn 
EXHKBIT DESCRIPTION/ TITLE 

NUMBER 

CX-060 GBT 2005 Interim Results 

CX-06 1 GBT Press Release 

(September 2005) 

(September 22,2005) 

PURPOSE 

Background, 

validity 

Background, 

validity 

SPONSORING 

WITNESS 

Stipulation of the 

Parties 

Stipulation of the 

Parties 

ADMITTED 

3/19/08 

31 19/08 

CX-062C 

CX-063 

CX-064 

Withdrawn 

Number intentionally not used 

Number intentionally not used 

cx-065 Withdrawn 

Validity 

CX-066 

CX-067 

CX-068 

CX-069 

CX-070 

CX-07 1 

CX-072 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

OHS West:260411067.2 

CX473 

ZX-074 

22 

1 

Number intentionally not used 

Number intentionally not used 

2X-075 

2x476 

JX-077 

Number intentionally not used 

Number intentionally not used 

Cowan et al., “Characterization of 

the Major Promoter for the PlasmidEncoded Sucrose Genes scrY, scrA, 

and scrB,” Journal of Bacteriology 

173(23):7464-7470 (199 1) 

1 Validity 

:X-078 

1x479 

Withdrawn 

Alaeddinoglu et al., “Transfer of a 

Gene for Sucrose Utilization into 

Escherichia coli K-12, and 

Consequent Failure of Expression of 

Genes for D-Serine Utilization,” 

Journal of General Microbiology 

110:47-59 (1979) 
EXHLBIT 

NUMBER 

cx-080 

Withdrawn 

Withdrawn I 

cx-08 1 

PURPOSE 

Validity 

DESCRIPTION/ TITLE SPONSORING 

WITNESS 

Garcia, “Cloning in Escherichia coli Liao 

and molecular analysis of the 

sucrose system of the Salmonella 

plasmid SCR-53,” Mol. Gen. Genet. 

Schmid et al., “Plasmid-Mediated 

Uptake and Metabolism of Sucrose 

by Escherichia coli K- 12.” Journal 

of Bacteriology 151(1):68-76 (1982) 

201575577 (1985) 

Validity 

Validity 

Liao 

Liao 

zx-090c 

3X-09 1C 

SX-092C 

JX-093C 

ZX-094C 

3X-095C 

CX-082 

CX-083 

CX-084 

CX-085 

CX-086C 

CX-087C 

ZX-088C 

ZX-089C 

Withdrawn 

Withdrawn . 

Scholle et al., “Expression and 

Regulation of a Vibrio alginolyticus 

Sucrose Utilization System Cloned 

in Escherichia coli,” Journal of 

Bacteriology 169(6): 2685-2690 

(1987) 

Number intentionally not used 

Withdrawn 

Number intentionally not used 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

IX-096C 

:X-O97C 

ZX-098C 

ZX-099C 

:X-lOOC 

:X- lOlC 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

ADMITTED 

3119108- 

3/19/08 

3/19/08 

OHS Wat:260411067.2 23 
EXHIBIT 

NUMBER 

DESCRIPTION/ TITLE PURPOSE SPONSORING ADMITTED 

WITNESS 

CX-129 1 

Withdrawn 

Nithdrawn 

Nithdrawn I 

cx-102c 

cx-103c 

cx-104c 

cx-105c 

CX- 106C 

CX-107C 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Respondents’ Supplemental 

Responses to Complainants’ 

Interrogatories Nos. 13, 14,19,20, 

52,54,57,58,65,68,78 and 83. 

Withdrawn 

Background, I Somerville I 3/19/08 

cx-108C 

Withdrawn 

Withdrawn 

cx- 109c 

cx-lloc 

Withdrawn 

Withdrawn 

CX-111c 

cx-112c 

cx-113c 

cx- 114c 

cx-115c 

CX-116C 

cx-117c 

cx-118C 

cx-119c 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

cx-12oc 

cx- 1 21 c 

Withdrawn 

Withdrawn 

cx-122c 

cx-123c 

CX- 124C Withdrawn 

CX- 125C Withdrawn ~ 

CX- 126C 

cx- 127c 

CX-128C 

Withdrawn 

Hithdrawn 

OHS Wcst2€f.J411067.2 24 
NUMBER 

CX-130 

cx-131c Validity Liao 3/19/08 

CX-132 Validity 

Validity 

DESCRIPTION/ TITLE 

Liao 3/19/08 

Liao 3/19/08 

Analyst report 

GBT communication with HSBC re: 

lysine business (GBT117650- 

(GBT088255-088260) 

1 17653, GBT 1 17846- 1 17849) 

~ 

CX-133 

CX- 134 

CX-135 

CX-136 

CX-137 

Analyst report 

(GBT163980- 163983) 

Analyst report 

Withdrawn 

Withdrawn 

GBT website content 

Number intentionally not used 

(GBT15172 1-151727) 

(GBT 174 16 1 - 174 168) 

Validity Liao 3/19/08 

CX-138 

CX- 139 

CX- 14OC 

CX- 14 1 

CX- 142 

CX- 143 

CX-144 

EX- 145 

Withdrawn 

GBT message to shareholders 

(GBT155240) 

Withdrawn 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

2X-15OC I Withdrawn 

Validity 

2X- 15 1 

Stipulation of the 3/19/08 

Parties 

Number intentionally not used 

EX- 146 

CIX- 147 

WITNESS 

Number intentionally not used 

Number intentionally not used 

EX- 148 

2X- 149 

Number intentionally not used 

Number intentionally not used 

OHS West26041 1067.2 25 
EXHIBIT 

NUMBER 

2X- 173 

SX- 174 

2X-175 1 

CX-155 

PURPOSE 

CX- 156C 

CX- 157 

CX-158 

CX- 159 

SPONSORING ADMITTED 

WITNESS 

CX- 160 

CX-161 

CX- 162 

CX-163 

cx-164 

Background, 

validity 

CX- 165 

cx- 166 ~~ 

CX- 167 Liao 3/19/08 

Background, Webb 

validity 

CX-168 

CX- 169 

3/19/08 

CX- 170 

CX-171 

EX-172 

DESCRWI’ION/ TITLE 

Number intentionally not used 

Withdrawn 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Number intentionally not used 

Withdrawn 

Withdrawn 

Withdrawn 

Number intentionally not used 

Withdrawn 

Halsall. D. M., “Overproduction of 

Lysine by Mutant Strains of 

Escherichia coli with Defective 

Lysine Transport Systems,” 

Biochemical Genetics, Vol. 13, Nos. 

112, (1975) 

Withdrawn 

Withdrawn 

Withdrawn 

Lemonnier, M., and Lane, D., 

“Expression of the second lysine 

decarboxylase gene of Escherichia 

Eoli,” Microbiology 144:751-760 

(1998) 

Withdrawn 

Vurnber intentionally not used 

Vumber intentionally not used 

rlumber intentionally not used 

‘I 

I I 

OHS Wat:260411067.2 26 
I cx-176c 

Withdrawn 

Withdrawn 

Number intentionally not used 

Withdrawn 

Withdrawn 

Withdrawn 

CV of Dr. James C. Liao 

Number intentionally not used 

List of items reviewed by Dr. James 

C. Liao 

Withdrawn 

Withdrawn 

cx- 177c 

CX-178C 

CX- 179C 

CX- 18OC 

CX- 18 1C 

CX- 182C 

CX-183C 

CX- 184 

CX- 185 

CX- 186 

CX- 187C 

CX-188C 

CX- 189 

cx-19oc 

cx-191c 

CX- 192C 

CX- 1 93 

CX- 194 

CX- 195 

CX- 196C 

CX- 197C 

Background, 

validity, 

enforceability 

Background, 

validity, 

enforceability 

validity 

Liao 

Liao 

Withdrawn 

3/19/08 

3/19/08 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

WITNESS 

Complainants 

I 

I 

I I 

OHS West26041 1067.2 27 
EXHIBIT DESCRIPTION/ TITLE PURPOSE 

NUMBER 

CX-202C Withdrawn 

CX-203 C Withdrawn 

CX-204C Withdrawn 

CX-205C Withdrawn 

CX-206C Withdrawn 

CX-207C Withdrawn 

CX-208C Withdrawn 

CX-209C Withdrawn 

CX-210C Withdrawn 

CX-211C Withdrawn 

CX-212C Withdrawn 

CX-213C Withdrawn 

CX-2 14C Withdrawn 

CX-215C Withdrawn 

CX-216C Withdrawn 

EX-2 17C Withdrawn 

“-2 18C Withdrawn 

ZX-219C Withdrawn 

JX-220C Withdrawn 

2X-22 1C Withdrawn 

ZX-222C Monthly Research Reports for Validity, 

2X-223C Withdrawn 

ZX-224C Withdrawn 

zX-225C Withdrawn 

:X-226 Number intentionally not used 

:X-227 Withdrawn 

:X-228 Withdrawn 

2X-229C withdrawn 

2X-230C Withdrawn 

0611994 (AHL 430694-99) enforceability 

OHS Wat:260411067.2 

SPONSORING ADMITTED 

WITNESS 

Joint Motion of the 3/26/08 

Parties 

28 
EXHIBIT I DESCRIlplrION/ TITLE I PURPOSE I SPONSORING I ADMITTED 

NUMBER 

CX-23 1C 

WITNESS 

Rebuttal Witness Statement of Validity, Liao 3/19/08 

.James C. Liao, Ph.D. enforceability 

CX-232C 

CX-233C 

CX-234C 

CX-235C 

CX-236C 

CX-237 

Stipulation of the 

Parties 

Rebuttal Witness Statement of Yuji 

Joe enforceability 

Rebuttal Witness Statement of Validity, 

Satoru Murao enforceability 

Rebuttal Witness Statement of Validity, 

Yoshimi Kikuchi enforceability 

Corrected Rebuttal Witness Validity, 

Statement of Hiroyki Kojima enforceability 

Withdram 

Kikuchi, et al., Biosc. Biotechnol. 

Biochem., 62 (6): 1267-1270,1998 

Unclean hands, 

Validity 

Stipulation of the 

Parties 

Kikuchi 

CX-238C 

CX-239 

CX-240C 

CX-241 C 

CX-242C 

Kojima 

I 

Withdrawn 

Transmissible Substrate-Utilizing Validity Kojirna 3/ 1 9/08 

Ability in Enterobacteria, Smith 

H.W. and Parsell Z., J. Gen. 

Microbiol. 1975; 87(1): 129-140 

Technology Research and Background, Stipulation of the 311 9/08 

Development Contract validity Parties 

Withdrawn 

Withdrawn 

(GBTZ 13396-2 13403) 

Kikuchi 

CX-243C 

CX-244C 

3/19/08 

I 

Withdrawn 

Withdrawn 

3/19/08 

CX-245 . 

EX-246C 

ZX-247C 

2X-248C 

3/14/08 

3/19/08 

311 9/08 

I 

Withdrawn 

Withdrawn 

Monthly Research Report for Validity, Koj ima 3/17/08 

1211992 (AHL 430789) enforceability 

(see also JX-091 C) 

Excerpt from 4th Research Report Validity, Kojima 3/19/08 

No. 11529 at AHL 435987 enforceability 

(see also JX- 127C) 

OHS Wu~Z60411067.2 29 
EXHIBIT 

NUMBER 

Validity, 

enforceability 

Unclean Hands; 

Obviousness 

CX-249C 

CX-25OC Kojima 31 19/08 

Stipulation of the 3/19/08 

Parties 

cx-251c 

Unclean Hands; 

Obviousness 

CX - 252C Stipulation of the 31 19/08 

Parties 

CDX-00 1C 

Validity, 

enforceability 

Validity, 

enforceability 

Validity, 

enforceability 

Val idit y, 

mforceabilit y 

CDX-002C 

CDX-003C 

CDXWC 

Liao 3/19/08 

Liao 3/19/08 

Liao 3/19/08 

Liao 3/19/08 

CDX-005C 

CDX-006 

CDX-007 

CDX-008C 

CDX-009C 

CDX-0 1 OC 

CDX-011 C 

CDX-012C 

CDX-013 

CDX-014 

2DX-015 

ZDX-0 16C 

DESCRIPTION/ TITLE 

Monthly Research Report for 

1211 993 (AHL 430733) 

(see also JX-06OC) 

Excerpt from 10th Lysine Project 

Research Report No. 11819 at AHL 

003173 

(see also JX-OSlC) 

Excerpts of Dehui Wang 

depositions of August 29,2007, 

August 30,2007 and August 3 1, 

2007 

Excerpts of Weigang Li deposition 

of October 24,2006 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

Withdrawn 

‘160 Patent Claims at Issue 

‘698 Patent Claims at Issue 

Partial List of Journal Articles on 

Sucrose Utilization Gene 

Excerpts from Deposition of 

Yoshimi Kikuchi 

OHS West:260411067.2 30 
EXHIBIT DESCRIPTION/ TITLE 

NUMBER 

PURPOSE SPONSORING ADMITTED 

WITNESS 

CDX-0 17C 

CDX-019 

CDX-020 

CDX-021 

CDX-022 

Withdrawn 

CDX-018 Comparison of small scale lab and Validity, Liao 3/19/08 

large scale fermenter enforceability 

Test tube, Lab-Flask, S-Jar 

Lysine fermenters 

Glucose and Sucrose Molecular 

Structure 

Feedback regulation of amino acid 

I Validity 

Glucose and sucrose molecular I cDx-025 I structures 

Validity, Liao 3/19/08 

enforceability 

Validity, Liao 3/19/08 

enforceability 

Validity, LBO 3/19/08 

enforceability 

Validity Kikuchi 3/19/08 

CDX-023 

biosynthesis pathways I 

AEC and lysine molecular Validity Kikuchi I 3/19/08 

CDX-024 

structures 

Glycolysis pathway Validity Kikuchi 31 19/08 

Kikuchi 

Kojima 

Kojima 

I I 

CDX-033 I Feedback inhibition in lysine I Validity 

3/19/08 

3/19/08 

311 9/08 

- 

I I 

CDX-034 I Feedback inhibition in lysine (2) 1 Validity 

CDX-026 

CDX-027 

I I 

CDX-035 I dapA gene Mutations I Validity 

Lysine biosynthesis pathway Validity 

Lysine degradation pathway Validity 

I I 

CDX-036 ] Rate limiting step 2 I Validity 

CDX-028 

CDX-029 

Kojima 31 19/08 

__ Chart showing rate limiting steps Validity Kojima 3/19/08 

Lysine biosynthesis pathway Validity Kojima 31 19/08 

Kojima 3/19/08 

CDX-030 

showing rate determining steps 

Plasmid Validity Kojima 311 9/08 

I I I I 

CDX-037 I Lysine and threonine production I Validity I Kojima I 3/19/08 

CDX-03 1 

CDX-032 

dapA gene sequence Validity 

dapA gene sequence with mutations Validity 

Kojima 

Kojima 

OHS Wcst:260411067.2 31 

3/19/08 

3/19/08 

CDX-038 

pathways 

Withdrawn 

CDX-039 Complainants' Demonstrative '160 Webb 3/19/08 

v. '765 Comparasion 
"Claim Is Best Mode '160 Timeline" 

PURPOSE 

I CDX-041 I Withdrawn 

SPONSORING ADMITTED 

WITNESS 

Webb 311 9/08 

Webb 31 19/08 

Webb 3/19/08 1 

CDX-042 1 Complainants' Demonstrative 

"Hypotheticals 1-5" 

CDX-043 Complainants' Demonstrative TA325 v. W-31 10 

CDX-044 Complainants' Demonstrative 

"Effect of LDC Knockout" 

CDX-045 Complainants' Demonstrative 

3/19/08 

3/19/08 

Webb 3/26/08 

OHS West:260411067.2 32 
UNITED STATES INTERNATIONAL TRADE COMMISSION 

Washington, D.C. 

Before The Honorable Charles E. Bullock 

CERTAIN L-LYSINE FEED PRODUCTS, 

THEIR METHODS OF PRODUCTION AND 

GENETIC CONSTRUCTS FOR 

PRODUCTION 

IN THE MATTER OF 

I~v. NO. 337-TA-571 

Lysine Decarboxylase Isolated from 

Escherichia colr" 

Kikuchi doctoral dissertation 

(AHL 431052-AHL 431 177) 

Pages from monthly reports, 10193 t 1 1/93 

(AHL 500025, AHL 500024) 

Exh. No. 

Rx 001 

unenforceability 

Invalidity, Webb or Kikuchi 

unenforceability 

Invalidity, Subject of 

unenforceability stipulation; Webb, 

Kojirna, Kikuchi, 

or Kawamura 

RX 002 

RX 003C 

RX 004c 

RX 005 

RX 006 

RX 007C 

RX 008C 

RX 009 

xx OlOC 

Nagano et al., "High Expression of the 

Second Lysine Decarboxylase Gene, Idc, in 

Escherichia coli W 196 Due to the 

Recognition of the Stop Codon (TAG), 

which Corresponds to the 33th Amino Acid 

Residue.. .I' 

Monthly Report 199 1 (August) 

(AHL 430843) 

(AHL 43 1040-AHL 43 1045) 

u( OllC 

Invalidity, 

unenforceability 

Invalidity, Subject of 

unenforceability stipulation; Webb, 

Kojirna, Kikuchi, 

or Kawamura 

RESPONDENTS' FINAL EXHIBIT LIST 

(AHL 430650-AHL 430656) 

(AHL 002505-AHL 002626) I unenforceability I 

Kikuchi et al., "Characterization of a Second I InvaIidity, I WebborKikuchi 

Kikuchi, Webb, or 

Somerville 

Ah itted 

03/17/08 

Admitted 

3/13/08 and 

03/17/08 

Admitted by 

Order No. 39 

dated 3/27/08 

Admitted 

031 1710 8 

Admitted 

3/13/08 and 

03/17/08 

Admitted 

3/13/08 and 

03/17/08 

Admitted 

03/ 19/08 

WITHDRAWN 

Admitted 

311 3/08 and 

0311 7/08 

Admitted by 

Order No. 39 

dated 3/27/08 

WITHDRAWN 
RXO13C I I 

RXO14C 1 

Rx 015c 

RX 016 GenBank Accession No. D49445 Invalidity 

RX 017 GenBank Accession No. M96394 Invalidity 

Rx 020 

Ronald L. Somerville, Ph.D CV 

I I 

RX 022 Number intentionally not used. 

RXO23C I I 

RXO24C I 

RX OZJC 

RX 026 NCBI printout re GenBank accession number 

AY48 5 1 5 0 

Doroshenko & Livshits, "Structure and mode 

of transposition of Tn2555 carrying sucrose 

utilization genes" 

One page computer print-out from 

Ajinomoto database re AJ13036 

RX 027 

RX 028C 

I (AHL500001) 

RXO29C I 

RXO3OC I 

Rx 031C 

RX 032C 

RX 033C 

RX 034C 

RX 035C 

RX 036C 

RX 037C 

RX 038C 

RX 039C Monthly Report -Kame Kawamura 

(AHL 4308 15) 

Invalidity, 

unenforceability 

Invalidity, 

unenforceability 

Invalidity, 

unenforceability 

Invalidity, 

unenforceability 

RXO4OC I I 

RX 041C 

RX 042C I 

RX 043C 

RX044cRX 045C 

RX 046C 

Webb, Somerville, 

Liao, or Blamer 

Webb, Somerville, 

Liao, or Blattner 

Ram 

Webb 

Somerville 

Kojima, Kikuchi, 

or Webb 

Kojima, Kikuchi, 

or Webb 

Kikuchi 

Subject of 

stipulation; Webb, 

Kojima, Kikuchi, 

or Kawamura 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

Admitted 

031 19/08 

Admitted 

03/19108 

Admitted 

03/19/08 

Admitted 

0311 9/08 

WITHDRAWN 

Admitted 

03/19/08 

Admitted 

3/13/08 and 

03/17/08 

Admitted 

03/19/08 

Admitted 

03/19/08 

03/19/08 

WITHDRAWN 

WITHDRAWN 

-2- 
WITHDRAWN 

WITHDRAWN 

RX 054C 

Unclean hands/ 

I 

Rx057C 

Admitted by 

RXO58C 1 

RX059C I 

RX 049C 

RX 050C 

RX 051C 

RXO6OC 1 

RX 061 I Number intentionally not used. 

Deposition designations, Atsushi Sasamori, 

__ 

RXO62C 1 

RX 063C 1 Strain development chart written by 

RX 069C 

RX 070C 

Rx 071C 

RX 072C 

RX 073C 

RX 074C 

1 Dr. Kikuchi it deposition I 

03/17/08 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

unen forceability 

Invalidity, 

unenforceability 

3/13/08 and 

0311 7/08 

Webb or Kikuchi Admitled 

3/13/08 and 

RX 064C 

unenforceability Order No. 39 

unenforceability Order No. 39 

Strain development chart 

(Am 430404) 

unenforceability I I 03/17/08 

I I WITHDRAWN 

RX 075C 

RX 076C - 

RX 077C 

Cleaning Ram Admitted 

Procedures/ 03/19/08 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

r WITHDRAWN WITHDRAWN 

. 

I 1 WITHDRAWN 

Invalidity, I Webb or Kikuchi I Admitted 

RX 065C 

RXO66C 

RX 067C 

RX 068C 

RX 078C 

RX 079C 

RX 080C 

Rx 08XC 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

-3- 
RX 082C 

RX 084C 

RX 087C 

6/16/06 

Complainant Ajinomoto Co., 1nc.k First 

Global Bio-Chem Technology Group 

Company Limited's First Set of 

Interrogatories (Nos. 1-43), dated 8/28/06 

Supplemental Responses to Respondent 

Rx 090c 

WITHDRAWN 

WITHDRAWN 

Invalidity, Ajinomoto Admitted 

Unclean hands' Shiroshita 

unenforceabilityl Webb 03/19/08 

WITHDRAW 

RX 097C 

Number intentionally not used. 

modified to reflect the stipulation) 

Witness Statement of Wang Dehui (to be Nai- wang 

Unclean hands, 

Cleaning 

proceduresISamp 

ling 

unen forceability 

Witness Statement of Ronald L. Somerville Invalidity, Somerville 

Witness Statement of Andrew C. Webb Invalidity, Webb I unenforceability I 

Complainant Ajinomoto Heartland LLC's I Invalidity, I Ajinomoto 

03/19/08 

03/14/08 

Admitted 

-4- 
Responses to Respondent Global Biochem 

Technology Group Company Limited's 

Fourth Set of Interrogatories (No. 641. dated 

RX 112c 

RX 113C 

RX 114C I E-Mail. Subject: After the Next Action Unenforceabilitv 

RX 11% 

I (Am33969 - AHL433970) 

RX 116C I (Letter) Would like to visit manufacturing I Unenforceability 

(AHL2129i8 - AHL212950) 

Agreement in the form of a letter that GBT 

will disclose to Ajinomoto information not 

available to the general public 

/ Unclean hands 

Unenforceability 

/ Unclean hands 

I (a33971) 

I Test of GBTs bacteria in August 2005, 

- 

sasamori 

Ajinomoto, 

sasamori 

/ Unclean hands 

/ Unclean hands 

facilities in Changchun for a better 

understanding of operations, re potential 

cooperation 

0311 9/08 

Admitted 

03/17/08 

RX 118C 

RX 11% 

FtX l20C 

RX 121C 

I (~~~433950 - m~43j95iE) i 

RX 122C I Japanese language document with English I Unenforceability 

(Excerpts) 

(AHIA21917 - AHL421985) 

Plant photos forwarded by K. Mulville in e- Unenforceability 

mail dated 7/19/07 / Unclean hands 

Itinerary for 4-7 Sept 2005 Ajinomoto Visit Unenforceability 

(AHL433941 -AHL433942) / Unclean hands 

Japanese language document with English Unenforceability 

translation. Document appears to be a draft / Unclean hands 

which served as the basis of the 9/16/2005 

meeting memo (Translator's note) 

(Translation, AHL43 3 949A-AHL43 3 949E) 

Japanese language document with English 

translation. GBT Plant Inspection Results 

Summary (Technical Aspects) 

Unenforceability 

/ Unclean hands 

Ajinomoto, 

Sasamori 

Ajinomoto, 

sasamori 

Ajinornoto, 

Sasamori 

Webb 

Admitted 

0311 7/08 

Admitted 

0311 9/08 

Admitted 

0311 7/08 

03/19/08 

Ajinomoto, 

Sasamori 

WITHDRAWN 

WITHDRAWN 

Aihomoto. Admitted 

Admitted 

031 17/08 

RX 123C 

RX 124C 

RX 125C 

RX 126C 

I 

Ajinomoto, I Admitted 

SaSamOri 

translation. Gallop Project Study T& 

Meeting Agenda, Bates Number 

Japanese language document with English 

banslation. Memo on Meeting with Global 

Bio-Chem Technology Group 

Japanese language document with English 

translation. Summary of Inspection of 

Global Bio-Chem Technology Group (Main 

Points) 

/ Unclean hand; 

(AHL435926- AHL435929E) 

Unenforceability 

/ Unclean hands 

(AHL433943 - AHL433945D) 

Unenforceability 

/ Unclean hands 

(GBT209748 - GBT209748C) 

Ajinomoto Response to GBT Fifth Set of Unenforceability 

Interrogatories (787107) / Unclean hands 

Ajinomoto Heartland LLC October Unen forceability 

Newsletter / Unclean hands 

(AHL294644-AHL294648) 

03/17/08 

Ajinornoto, 

Sasamori 

Aj inornoto, 

sasamori 

SaSamori 03/17/08 

Admitted 

03/17/08 

Admitted 

03/17/08 

Ajinomoto, Admitted 

sasamori 0311 7/08 

Ajinomoto. Admitted 

03/17/08 

Ajinomoto, Admitted 

0311 7/08 

I 

-5- 
'Exh.<No.- TI 

RX 127C 

RX l28C 

Rx 129c 

RX 130C 

RX 131C 

RX 132C 

RX 133C 

RX 134C 

RX 135C 

RX 136C 

RX 137C 

RX 138C 

RX 139C 

RX 140C 

RX 141C 

Japanese language document with English 

translation. Management Conference Report 

Materials; Global Bio-Chem Technology 

Group (GBr) Inspection Report 

(Am433938 -A€€L433939D) 

E-mail 

Subject Samples of GBT Lysine 

(AHL 241941) 

E-mail 

Subject: RE: Samples of GBT Lysine 

(purchased fkom Wholesale Feed in Iowa) 

Analysis of Dahe Samples 

Email subject re September visit to facilities 

in Changchun and Dehui 

(AHL433972) 

Japanese language document with English 

translation. Gallop Project Kick-Off Meeting 

- Minutes, Bates Number 

(AHL 291 5 16 - AHL 29 15 17) 

(AHLA35917 - AHL435925J) 

Letter, subject re: Visit to Changchun and 

Dehui production sites 

(AHL433973) 

E-mail 

Subject: FW. PCR Analysis in USA 

(AHL 415915A) 

Japanese language document with English 

translation. Minutes of Gallop Study Team 

Meeting, 

Japanese language document with English 

translation. Regarding Gallop Project 

E-mail 

Subiect: FW PCR Analysis in USA 

(Am435930 -AHL435932D) 

(AHL433954 - AHL433955C) 

(AHL 4 I5890A - AHL 41 5891A) 

Iauanese languae document with English 

&slation. :-Gail, Subject: Gallop Project 

Update (Confidential) 

;AHL433956) 

E-mail 

Subject: Strategy Meeting 

[AHL 296290) 

lapanese language document with English 

mslation. Gallop Project Update 

:Confidential) 

lAHL433957 - AHL433957C) 

Unenforceability 

/ Unclean hands 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unen forceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

men forceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Ajinornoto, 

Shiroshita 

Ajinomoto, 

Maxwell 

Ajinomoto, 

Maxwell 

Ajinomoto, 

Shiroshita 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Maxwell 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Maxwell 

Ajinomoto, 

Shiroshita 

Ajinomoto, 

Maxwell 

Ajinomoto, 

Sasamori 

WITHDRAWNAdmitted 

0311 9/08 

Admitted 

03/17/08 

Admitted 

03/19/08 

Admitted 

03/17/08 

Admitted 

0311 7/08 

Admitted 

031 17/08 

Admitted 

0311 7/08 

Admitted 

03/17/08 

Admitted 

0311 7/08 

Admitted 

0311 7/08 

Admitted 

03/19/08 

Admitted 

03/17/08 

Admitted 

0311 9/08 

Admitted 

03/17/08 

-6- 
Exh. No, Descriptio-tle . .. 

Ajinomoto, 

Sasamori 

Aj inomoto, 

Sasamori 

I -33967C) 

RX 15OC 1 Japanese language document with English 

Admitted 

031 1 7/08 

Admitted 

03/17/08 

RX 144C 

RX 145C 

RX146C 

RX 147C 

(AHL435916-AHL435916C) 

Japanese language document with English 

translation. E-mail, Subject: Gallop Update 

(Confidential) 

(AHL433961-AHL43396 1 B) 

AAN Strategy Meeting 2005 Manual (12/7- 

8/2005) Final 

E-mail 

Subject: RE: potential FCR lab 

(AHL 416650A) 

Preliminary Information Request List 

(AHL433964 - AHIA33965) 

(AHL179628-AHL179647) 

Purpose ';* 

Ajinomoto, 

Sasamori 

Ajinomoto, 

sasamori 

.e 

Unclean hands/ 

unenforceability 

Admitted 

0311 7/08 

Admitted 

0311 7/08 

Unclean hands/ 

unenforceability 

Unclean handd 

unenforceability 

RX 148C 

RX 149C 

Unclean hands/ 

unenforceability 

Unclean handd 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

men forceability 

Japanese language document with English 

translation. E-mail, Subject: Gallop Project 

Update (Confidential) 

Japanese language document with English 

translation. E-mail, Subject: Gallop Update 

(Confidential), (MIA33966 - 

(AHL433952 - AHL433953D) 

Unclean hands/ 

unenforceability 

RX 151C 

FtX 152C 

RX 153C 

RX 154C 

RX 155C 

Unclean hands/ 

&slation. Minites of Gallop Study?eam unenforceability 

Meeting 

Japanese language document with English 

Wslation. Gallop Project Study Team 

Meeting Materials (Confidential) 

Ajinomoto Response to Interrogatory No. 42 

(6116106) 

Ajinomoto Co., Inc. Annual Report 2006 

Monthly Director's Meeting Minutes April 7, 

E-mail, Subject: Gallop final 

(AHL435940 - AHL435941C) 

(Am435938 - AHL435939C) 

2006 (AHL436328- AHL436333) 

IAHL433978 - AHL433979D) 

Unclean hands/ 

unen forceability 

Sasamori 

Unclean hands/ 

unen forceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unenforceability 

Unclean hands/ 

unen forceability 

Unclean hands/ 

unenforceability 

Sasamori 

Unclean hands/ 

unen forceability 

Ajinomoto 

Ajinomoto, 

Sasamori 

Aj inomoto, 

Maxwell 

Ajinomoto, 

Sasamori 

Ajinomoto, 

Shiroshita 

Aj inornoto, 

Sasamori 

Sasamon 

Admitted 

0311 7/08 

Admitted 

0311 9/08 

Admitted 

0311 9/08 

Admitted 

03/17/08 

Admitted 

0311 7/08 

Admitted 

031 19/08 

RX 156C 

3X 157C 

Sasamori 03/19/08 

Ajinomoto, Admitted 

Maxwell 0311 9/08 

Japanese language document with English 

translation. Explanation Concerning Lysine 

Product Sample (Crystal Lysine) 

(GBT209749A 4BT209750A) 

Japanese language document with English 

translation. Declaration of Masahiro 

Yamada with respect to project at Ajinomoto 

Co., Ltd. for purchasing Global Bio-Chem 

(GBT209746 - GBT209747C) 

Ajinomoto, 

Sasamori 

Admitted 

03/17/08 03/17/08 

0311 7/08 

03/17/08 

-7- 
Microorganisms," Microbiol. Rev. 49:8 1-99 

RX 172 

RX 173C 

RX 174 

RX I75C 

RX 176C 

Rx 177C 

RX 167 WITHDRAWN 

RX 168 GBTs Notice of Deposition to Ajinomoto Invalidity, Kojima, Kikuchi, Admitted 

unenforceabilityl Maxwell, 03/19/08 

Unclean hands Shiroshita, 

I WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

Number intentionally not used. 

FDA documents 1 Invalidity, Webb, Kojima, 1 Admitted 

I I I I I 

RX169C I I I WITHDRAWN 

RX 17OC I "Mutation Analysis of the Feedback I Invalidity I Kojima I Admitted 

Inhibition Site of Aspartokinase 111 of 

Escherichia coli K-12 and its Use in LThreonine Production" by Ogawa-Miyata, 

031 19/08 

iima & Sano 

-8- 
RX 196 

RX 197 

Number intentionally not used. 

10/13/06 Response to office Action in file Invalidity Kojima, Kikuchi, Admitted 

history of U.S. Patent No. 7,179,623 Webb, or 3/13/08 and 

I I Interrogatories Nos. 66-7 1 I unenforceability I 

I SomerviIle 03/17/08 

, RX 198 WITHDRAWN 

RX 199C WITHDRAWN 

RX 200c WITHDRAWN 

RX 201c WITHDRAWN 

Rx 202 WITHDRAWN 

RX 203C Complainants' Answers to Respondents' Invalidity, ' Ajinomoto Admitted 

1 765 patent showing its assignmenUlicense to unenforceability witness; Webb, I Ajinomoto I I Somerville, or 

RX 226 

RX 227C 

RX 228C 

Rx 229 

Rx 230 

RX 231 

Kojima 

Number intentionally not used. 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

Number intentionally not used. 

-9- 

1 
233 

Repression of Aspartic Semialdehyde 

Dehydrogenase in Escherichia coli K- 12," .l 

Bacteriol. 1 12234-92 ( 1972) 

U.S. Patent No. 3,580,810 Invalidity, 

unenforceability 

a 236C 

RX 237C 

RX 238C 

RX 234 

RX 235 

Rx239C I 

RX24OC I 

U.S. PatentNo. 7,179,623 Invalidity 

RX 242C 

RX 243C 

RX 244 Kashiwagi, K. et al., "Coexistence of the Invalidity 

Invalidity 

RX 245 

RX 246 

Genes for Putrescine Transport Protein and 

Ornithine Decarboxylase at 16 min on 

Escherichia coli Chromosome," J. Biol. 

Chem. 266,20922-7 (199 1) 

Doroshenko, V. G. et al., "Structural and 

functional organization of the transposon 

Tn2555 carrying saccharose utiliZatjon 

RX249 I I 

RX250 1 

RX 247 

RX 24R 

RX252 I I 

RX253 I 

genes," Mol.-BGl. 22:645-658 (1 988) 

Number intentionally not used. 

RX254 I 

RX 255C I Witness statement of Neil M. Ram, Ph.D., 

RX 256C 

Remedy and 

LSP, CHMM bonding 

Witness Statement of Li Weigang Unclean hands ' RX 257C 

RX 258C 

RX 259C 

RX 260C 

RX 261 

iO/2005 AHL Sales & Marketing report Unclean hands/ 

(AHL 193726193733) (Formerly JX 18lC) Unenforceability 

10/2005 AHL Newsletter Unclean hands/ 

(AHL 294644-294648) (Formerly JX 182C) Unenforceability 

1 lDOO5 AHL Sales & Marketing report Unclean hands/ 

(AHL 193717-193725) (Formerly JX 183C) Unenforceability 

132005 AHL Sales & Marketing report Unclean hands/ 

(AHL 193710-193716) (Formerly JX 184C) Unenforceability 

~~ 2006 Aiinomoto Investors' Guide (Formerly Unclean hands/ 

RX 262C 

-Spoioring . -* wiia : 

Webb, Somerville, 

Liao, or Blattner 

Jx l8Sj Unenforceability 

04/2006 AHL Sales & Marketing Report Unciean hands/ 

Kojima or Webb 

(AHL. 4361 93-436202) (Formerly JX 186C) 

Kojima, Kikuchi. 

Webb, or 

Sornerville 

Unenforceability 

Webb, Sornerville, 

Liao, or Blattner 

Webb, Sornerville, 

Liao, or Blattner 

Ram 

Li 

Sasamori 

Ajinomoto 

sasamori 

Ajinomoto 

sasamori 

Ajinomoto 

sasamori 

Aj inomoto 

sasamori 

Aiinomoto 

Maxwell 

Ajinomoto 

Admitted 

0311 9/08 

Admitted 

03/19/08 

WITHDRAWN 

Admitted 

3f 13/08 and 

03/17/08 

WITHDRAWN 

Admitted 

03ii9ioa 

WITHDRAWN 

Admitted 

0311 9/08 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

Admitted 

03/19/08 

Admitted 

0311 9/08 

Admitted 

03/19/08 

Admitted 

03/19/08 

Admitted 

03/19/08 

Admitted 

03/19/08 

Admitted 

0311 9/08 

Admitted 

03/19/08 

- 10- 
r 

'765 Patent Double-Patenting Chart 

RX 264 

RX 265 

RX 266 

Purppse 

Background 

Rx-268 r 

Sphnsoririg - 

: Witness,. - 

Kawamura 

RPX sc 

RPX 7c 

RPX 8C 

RDX-1c 

nvalidity 

RDX-2c tWebb, Somerville 

F RDx-3c RDX-4c 

t RDX-5c 

RDX-6C 

RDX-7c 

I RDX-9 

RDX-10c 

RDX-15 

DescriptiotuTiile ; '. 

Article - Breeding of Phenylalanineproducing Brevibucteriurnjlavum Strains by 

Removing Feedback Regulation of Both the 

Two Key Enzymes in Its Biosynthesis 

Authors: Shuo, Sugimoto & Kawamura 

GenBank Accession No. D49445 (printed 

2/19/2008) 

Unclean hands timeline 

Best mode/inequitable conduct timeline for 

claim 15 of '160 patent 

Number intentionally not used. 

Best moddiequitable conduct timeline for 

claim 22 of'160 patent 

Best modelinequitable conduct timeline for 

claim 13 of '698 patent 

Lysine Biosynthesis and Decomposition 

slides 

Host Cells and Plasmids slides 

Maxwell. 

Shiroshito, 

Invalidity, I Webb,Kojima, 

unenforceability Kawamura, 

Kikuchi, 

Nakanishi, Murao 

Unenforceability Webb, Kojima, 

Kawamura, 

Kikuchi, 

Nakanishi, Murao 

Kawamura, 

Kiuchi, 

Nakanishi, Murao 

Unenforceability Webb, Kojima, 

I 

hvalidity , I Webb, Sornerville 

inenforceability 

:nvalidity , 1 Webb, Somerville 

inenforceability 1 

I 

I 

I I 

I I 

- 11 - 

' status ' 

Admitted 

0311 7/08 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

Admitted by 

Order No. 39 

0311 9/08 

0311 9/08 

0311 9/08 

031 19/08 

WITHDRAWN 

Admitted 

03/19/08 

Admitted 
*e Purpose -' . I Exh. No. I Descriptioflitle Sponsoring 

' WitneWebb, Somerville 

Webb 

Webb, Somerville 

., ,I I I RDX-18C 1 Importance of Host Sdain Slides I Invalidity, 

Status 

Admitted 

03/19/08 

Admitted 

03/19/08 

Admitted 

RDX-19C 

RDX-ZOC _. I Undisclosed Strains Slides I unenforceability 

RDX-21 I AEC Selection Slides I Invalidity. 

unenforceability 

Invalidity, 

Number intentionally not used. 

Lysine Production of Disclosed vs. 

RDX-25c 

Kawamura, 

Kikuchi, 

Nakanishi, or 

Webb 

Koj ha, 

Kawamura, Webb, 

Somerville 

Kojima, Kikuchi, 

Webb, SomeMlle 

RDX-27C 

RDX-28C 

RDX-29c 

03/19/08 

WITHDRAWN 

WITHDRAWN 

Admitted 

03/19/08 

Admitted 

03/19/08 

WITHDRAWN 

WITHDRAWN 

WITHDRAWN 

RDX-30C 

RDX-31C 

RDX-32C RX 97 slides Invalidity, 

RDX-33c 

RDX-34c 

RDX-35C 

RDX-36C 

RDX-37c 

RDX-38C 

RDX-39c 

unenforceability 

'160 patent timeline document call-out slides 

(highlighting particular documents used to 

construct timelines) 

'698 patent timeline document call-out slides 

(highlighting pdcular documents used to 

construct timelimes) 

Invalidity, 

unenforceability 

Invalidity, 

unenforceability 

103/19/08 I 

Dated: April 4,2008 Respecti?& submitted, 

ADDUCI, MASTRIANI & SCHAUMBERG, L.L.P. 

1200 Seventeenth Street, N.W., Fifth Floor 

Washington, DC 20036 

Telephone: (202) 467-6300 

- 12- 
1. Deposition Exhibit to Trial Exhibit Cross Reference 

RX 118 RX 115C 

RX 119 RX 119C 

Rx 120 RX 120 

Rx 121 RX 123C 

RX 122 Rx 121 

RX 123 RX 128C 

RX 124 RX 139C 

RX 126 RX 156C 

RX 128 RX 131C 

RX 130 RX 133C 

RX 132 RX 137C 

RX 133 RX 261 

RX 134 RX 158C 

RX 135 RX 159C 

RX 136 RX 257C 

RX 137 RX 259C 

RX 138 RX 260C 

RX 139 RX 145C 

RX 140 RX 114C 

RX 141 RX 116C 

RX 142 RX 117C 

RX 143 RX 124C 

RX 145 RX 132C 

RX 146 RX 134C 

RX 147 Rx 122c ,f 

RX 151 RX 126C 

RX 151 RX 258C 

RX 152 RX 153 

RX 153C RX 136C 

RX 154C RX 147C 

RX 155C RX 141C 

RX 156C RX 142C 

RX 161C I Rx 143C 

RX 163C 1 RX 144C 

RX 166C RX 148C 

RX 167C RX 149C 

RX 168C RX 150C 

RX 169C RX 151C 

a. Exhibits Entered by Stipulation or Agreement 

RX 170C 

RX 173C 

Rx 155C 

FX 157C 
Rx 196C 

Rx 197C 

Rx 200c 

RX 201c 

RX 138C 

RX 135C 

RX 154C 

RX 262C 

RX 191c 

RX 140C 

RX 208C 

RX 216C 

RX-114 

Rx-115 

RX-117 

b. Deposition Exhibits Referenced at Hearing 

RX 146C 

RX 125C 

RX-168 

Rx-09OC 

RX-093C 

RX 001 

RX 002 

RX 008 

NO11 

RX 031 

RX 051 

RX 064 

Rx 76 

RX 82 

2. RX Exhibit Replaced by Duplicative JX Exhibit 

Xl 

Jx2 

RX2 

Jx 11c 

JX 15C 

JX 51C 

RX 64C 

JX 50C 

Jx 82 C 

Respondents' Exhibit RX-36 was among exhibits made defunct by a joint exhibit 

(JX) agreed to and admitted on the final day of hearing March 19,2008, specifically, JX199c. 

DACH200008-Final-add 
IN THE MATTER OF CERTAIN L-LYSINE FEED 

PRODUCTS, THEIR METHODS OF PRODUCTION AND 

GENETIC CONSTRUCTS FOR PRODUCTION 

337-TA-571 

CERTIFICATE OF SERVICE 

I, Marilyn R. Abbott, hereby certify that the attached ORDER was served upon, Juan S. 

Cockburn, Esq., Commission Investigative Attorney, and the following parties via first class 

mail and air mail where necessary on August 15 ,2008. 

U.S. International Trade Commission 

500 E Street, S.W., Room 112A 

Washington, DC 20436 

FOR COMPLAINANT AJINOMOTO HEARTLAND LLC: 

Raymond G. Mullady, Jr., Esq. 

Joseph M. Malkin, Esq. 

David E. Wong, Esq. 

Xue Wang, Esq. 

Yazhe Liu, Esq. 

Carrie Yizhi Wang, Esq. 

Sun Jing, Esq. 

Jason Zhijun Lin, Esq. 

ORRICK, HERRINGTON, & SUTCLIFFE LLP 

Columbia Center 

1152 15~ Street, N.W. 

Washington, DC 20005- 1706 
IN THE MATTER OF CERTAIN L-LYSINE FEED 

PRODUCTS, THEIR METHODS OF PRODUCTION AND 

GENETIC CONSTRUCTS FOR PRODUCTION 

337-TA-571 

FOR RESPONDENTS GLOBAL BIO-CHEM TECHNOLOGY GROUP COMPANY 

LIMITED; CHANGCHUN DACHENG BIO-CHEM ENGINEERING 

DEVELOPMENT CO., LTD.; CHANGCHUN BAOCHENG BIO-CHEM 

DEVELOPMENT CO., LTD.; CHANGCHUN DAHE BIO TECHNOLOGY 

DEVELOPMENT CO., LTD. & BIO-CHEM TECHNOLOGY (HK) LIMITED 

Tom M. Schaumberg, Esq. 

Sarah E. Hamblin, Esq. 

ADDUCI, MASTFUANI & SCHAUMBERG, L.L.P. 

1200 Seventeenth Street, N.W. 

Fifth Floor 

Washington, DC 20036 

PUBLIC MAILING LIST 

Sherry Robinson 

8891 Gander Creek Drive 

Miamisburg, OH 45342 

LEXIS - NEXIS 

Kenneth Clair 

THOMSON WEST 

1 100 - 1 3'h Street NW 

Suite 200 

Washington, DC 20005 

certain L-lysine feed products and genetic constructs for production thereof by reason of 

infringement of claims 13, 15-19, and 21-22 of U.S. Patent No. 5,827,698 ("the '698 patent") 

and claims 1,2, 15, and 22 of U.S. Patent No. 6,040,160 ("the '160 patent"). The complaint 

further alleges that an industry in the United States exists as required by subsection (a)(2) of 

section 337. Global Bio-Chem Technology Group Company Ltd. of Hong Kong; Changchun 

Dacheng Bio-Chem Engineering Development Co., Limited; Changchun Baocheng Bio-Chem 

Development Co., Ltd; Changchun Dahe Bio Technology Development Co. Ltd., all of China, 

and Bio-Chem Technology (HK) Limited of Hong Kong were named respondents in the 

investigation. Id. On June 29,2006, complainant Heartland filed a motion to amend the 

complaint to add its parent company, Ajinomoto, Inc., as a complainant. The motion was 

granted. No petitions for review were filed and the Commission determined not to review that 

ID. 

On April 30,2007, the ALJ issued an ID extending the target date of this investigation by 

twelve months to July 30,2008 (26 months), and the deadline for his final ID to March 3 1,2008. 

No petitions for review were filed and the Commission did not review this determination. 

On August 10,2007, the ALJ issued the subject ID (Order No. 17) terminating this 

investigation in part, pursuant to Commission Rule 2 10.2 1 (a)( l), with respect to claims 1,2, and 

22 of the ' 160 patent and claims 13, 16- 19, and 2 1-22 of the '698 patent. No petitions for review 

of the ID were filed, and the Commission has determined not to review the ID. 

The authority for the Commission's determination is contained in section 337 of the 

Tariff Act of 1930, as amended (19 U.S.C. 0 1337), and in sections 210.21,210.42 of the 

Commission's Rules of Practice and Procedure (19 C.F.R. $5 210.21,210.42). 

By order of the Commission. 

Marilyn R. Abdad 

Secretary to the Commission 

Issued: August 29,2007 

2 
CERTAIN L-LYSINE FEED PRODUCTS, THEIR METHODS 337-TA-571 

OF PRODUCTION AND GENETIC CONSTRUCTS FOR 

PRODUCTION 

CERTIFICATE OF SERVICE 

I, Marilyn R. Abbott, hereby certify that the attached NOTICE OF COMMISSION 

DECISION NOT TO REVIEW AN INITIAL DETERMINATION 

TERMINATING THE INVESTIGATION IN PART has been served by hand upon 

the Commission Investigative Attorney Juan S. Cockburn, Esq., and the following parties 

as indicated, on &ust 30. 7007 . 

Marilyn R. AbMtt, d&&- 

Secretary 

U.S. International Trade Cokission 

500 E Street, SW 

Washington, DC 20436 

ON BEHALF OF COMPLAINANT AJINOMOTO 

HEARTLAND LLC AND AJINOMOTO, INC.: 

Frank R. Samolis, Esq. 

PATTON BOGGS LLP 

2550 M Street, NW 

Washington, DC 20037 

P-202-457-6000 

Marc R. Labgold, Ph.D. 

Kevin M. Bell, Esq. 

Scott A.M. Chambers, Ph.D. 

PATTON BOGGS LLP 

8484 Westpark Drive, 9th Floor 

McLean, Virginia 22 102 

P-703-744-8000 

F-703-744-800 1 

Raymond G. Mullady, Jr. 

ORRICK, HERRINGTON & SUTCLIFFE LLP 

Washington Harbour 

3050 K Street, NW 

Washington, DC 20007 

P-202-339-8400 

F-202-339-8500 

( ) Via Hand Delivery 

(.(Via Overnight Mail 

( ) Via First Class Mail 

( )Other: 

( ) Via Hand Delivery 

(*Via Overnight Mail 

( ) Via First Class Mail 

( )Other: 

(%a Hand Delivery 

(I ia Overnight Mail 

( ) Via First Class Mail 

( )Other: 
Page 2 - Certificate of Service 

Joseph M. Malkin, Esq. 

ORRICK, HERRINGTON & SUTCLIFFE LLP 

The Onick Building 

405 Howard Building 

San Francisco, CA 94105 

P-415-773-5505 

F-415-773-5759 

James C. Brooks, Esq. 

Kurt T. Mulville, Esq. 

David E. Wang, Esq. 

ORRICK, HERRINGTON & SUTCLIFFE LLP 

4 Park Plaza, Suite 1600 

Irvine, CA 92614-2558 

P-949-567-6700 

F-949-567-6710 

ON BEHALF OF RESPONDENTS GLOBAL BIOCHEM TECHNOLOGY GROUP COMPANY 

ENGINEERING DEVELOPMENT CO., LTD., 

DEVELOPMENT CO., LTD., CHANGCHUN DAHE 

BIO TECHNOLOGY DEVELOPMENT CO., LTD., 

LIMITED, CHANGCHUN DACHENG BIO-CHEM 

(CHANGCHUN BAOCHENG BIO-CHEM 

AND BIO-CHEM TECHNOLOGY LIMITED: 

Tom M. Schaumberg, Esq. 

Michael G. McManus, Esq. 

Sarah E. Hamblin, Esq. 

ADDUCI, MASTRIANI & SCHAUMBERG LLP 

1200 Seventeenth Street, NW 

Fifth Floor 

Washington, DC 20036 

P-202-467-6300 

F-202-466-2006 

Mitchell J. Matorin, Esq. 

Clarie Laporte, Esq. 

DeAnn Smith, Esq. 

FOLEY HAOG LLP 

Seaport World Trade Center West 

155 Seaport Blvd. 

Boston, MA 022 10-2600 

P-617-832-1000 

F-617-832-7000 

( ) Via Hand Delivery 

(qia Overnight Mail 

( ) Via First Class Mail 

( )Other: 

( ) Via Hand Delivery 

( fiia Overnight Mail 

( ) Via First Class Mail 

( )Other: 

( ) Via Hand Delivery 

( $&a Overnight Mail 

( ) Via First Class Mail 

( )Other: 

( ) V'.a Hand Delivery 

( $ 4 ia Overnight Mail 

( ) Via First Class Mail 

( )Other: