Original Papers (only)< Year 2000 >Nogi T., Kobayashi M., Nozawa Y., and Miki K.: “Crystallization and preliminary crystallographic
analysis of high-potential iron-sulfur protein from Thermochromatium tepidu”, Acta Cryst. D56, 656-658(2000).
Mizuno N., Hittel D. S., Miki K., Voordoaw G., and Higuchi Y.: “Preliminary X-ray crystallographic
studies of DsrD protein from the sulfate-reducing bacterium Desulfovibrio vulgaris”, Acta Cryst. D56,754-755 (2000).
Park S.-Y., Yamane K., Adachi S., Shiro Y., Weiss K. E., and Sligar S. G.: “Crystallization andpreliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricu”,Acta Cryst. D56, 1173-1175 (2000).
BL44B2Sun D., Sato M., Yoshida T., Shimizu H., Miyatake H., Adachi S., Shiro Y., and Kikuchi A.:“Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase”, Acta Cryst. D56,1180-1182 (2000).
BL44B2
Yamada S., Park S.-Y., Shimizu H., Koshizuka Y., Kadokura K., Satoh T., Suruga K., Ogawa M., IsogaiY., Nishio T., Shiro Y., and Oku T.: “Structure of cyochrome c6 from the red alga Porphyra yezoensis at
1.57Å resolution”, Acta Cryst. D56, 1577-1582 (2000).
BL44B2Isogai Y., Ishii A., Fujisawa T., Ota M., and Nishikawa K.: “Redesign of artificial globins : Effects ofresidue replacements at hydrophobic sites on the structural properties”, Biochemistry 39, 5683-5690(2000).
BL45XU
Noguchi T., and Sugiura M.: “Structure of an active water molecule in the water-oxidizing complex ofphotosystem II as studied by FTIR spectroscopy”, Biochemistry 39, 10943-10949 (2000).
Gibney B. R., Isogai Y., Rabanal F., Reddy K. S., Grosset A. M., Moser C. C., and Dutton P. L.:“Self-assembly of heme A and heme B in a designed four-helix bundle: Implications for a cytochrome coxidase maquette”, Biochemistry 39, 11041-11049 (2000).
Mukai M., Nakamura K., Nakamura H., Iizuka T., and Shiro Y.: “Roles of IIe209 and IIe210 on the heme
pocket structure and regulation of histidine kinase activity of oxygen sensor FixL from Rhizobium
meliloti”, Biochemistry 39, 13810-13816 (2000).
Shen J., and Kamiya N.: “Crystallization and the crystal properties of the oxygen-evolving photosystem IIfrom Synechococcus unlcanus”, Biochemistry 39, 14739-14744 (2000).
Yamada S., Nakamura T., Tanaka Y., Isogai Y., Nishio T., and Oku T.: “Characterization and amino acidsequences of cytochromes c6 from two strains of the green alga Chlorella vulgaris”, Biosci. Biotechnol.
Biochem. 64, 628-632 (2000).
Furuichi M., Nishimoto E., Koga T., and Yamashita S.: “Time-resolved fluorescence studies on theinternal motion of LHCII in lipid membranes”, Biosci. Biotechnol. Biochem. 64, 1623-1627 (2000).
Fukai S., Nureki O., Sekine S., Shimada A., Tao J., Vassylyev D.G., and Yokoyama S.: “Structural basisfor double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNAValand valyl-tRNA synthetase”, Cell 103, 793-803 (2000).
BL44B2Bolze J., Fujisawa T., Nagao T., Norisada K., Saito H., and Naito A.: “Small angle X-ray scattering andP NMR studies on the phase behavior of phospholipid bilayered mixed micelles”, Chem. Phys. Lett. 329,215-220 (2000).
BL45SAXS

31Tsukihara T., and Aoyama H.: “Membrane protein assemblies-towards atomic resolution analysis”, Curr.
Opin. Structural Biol. 2000 10, 208-212 (2000).
Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., and Kuramitsu
S.: “Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme
thermophile, Thermus thermophilus HB8”, EMBO J. 19, 3857-3869 (2000).
BL45XU
Sano K., Maeda K., Taniguchi H., and Maéda Y.: “Amino acid replacements in an internal region oftropomyosin alter the properties of the entire molecule”, Eur. J. Biochem. 267, 4870-4877 (2000).
Kostyukova A., Maeda K., Yamauchi E., Krieger I., and Maéda Y.: “Domain structure of tropomodulin;
Distinct properties of the N-terminal and C-terminal halves”, Eur. J. Biochem. 267, 6470-6475 (2000).
Iwamoto H., Suzuki T., and Fujisawa T.: “Time-resolved two-dimensional X-ray diffraction study of theeffect of shortening on activation of contracting skeletal muscle”, Eur. J. Physiol. 439, 646-649 (2000).
BL45SAXS.
Kato R., Kataoka M., Mikawa T., Masui R., Nakagawa N., Kamikubo H., and Kuramitsu S.:“Observation of RecA protein monomer by small angle X-ray scattering with synchrotron radiation”,FEBS Lett. 482, 159-162 (2000).
Mishima M., Hatanaka M., Yokoyama S., Ikegami T., Wälchli M., Ito Y., and Shirakawa M.:“Intermolecular 31P-15N and 31P-1H scalar couplings across hydrogen bonds formed between a protein anda nucleotide”, J. Am. Chem. Soc. 122, 5883-5884 (2000).
Hirao I., Otsuki T., Mitsui T., and Yokoyama S.: “Dual specificity of the pyrimidine analogue,4-methylpyridin-2-one, in DNA replication”, J. Am. Chem. Soc. 122, 6118-6119 (2000).
Fujisawa T., Inoue K., Oka T., Iwamoto H., Uruga T., Kumasaka T., Inoko Y., Yagi N., Yamamoto M.,
and Ueki T.: “Small-angle X-ray scattering station at the SPring-8 RIKEN beamline”, J. Appl. Crystallogr.
33, 797-800 (2000).
BL45SAXS
Sugahara M., Mikawa T., Kato R., Fukuyama K., Kumasaka T., Yamamoto M., Inoue Y., and Kuramitsu
S.: “Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM
protein involved in repairs of oxidative DNA damage”, J. Biochem. 127, 9-11 (2000).
BL45XUKukimoto M., Nureki O., Shirouzu M., Katada T., Hirabayashi Y., Sugiya H., Furuyama S., Yokoyama S.,
and Hara-Yokoyama M.: “Crystallization and preliminary X-ray diffraction analysis of the extracellulardomain of the cell surface antigen CD38 complexed with ganglioside”, J. Biochem. 127, 181-184 (2000).
Uga H., Komori H., Miki K., and Wada C.: “The iteron regions necessary for the RepE-iteron interaction
In vivo in Mini-F plasmids of Escherichia coli”, J. Biochem. 127, 537-541 (2000).
Kimura M., Sekido S., Isogai Y., and Yamaguchi I.: “Expression, purification, and characterization ofblasticidin S deaminase (BSD) from Aspergillus terreus: The role of catalytic zinc in enzyme structure”, J.
Biochem. 127, 955-963 (2000).
Sano K., Maeda K., Oda T., and Maéda Y.: “The effect of single residue substitutions of serine-283 on thestrength of head-to-tail interaction and actin binding properties of rabbit skeletal muscle α-tropomyosin”,J. Biochem. 127, 1095-1102 (2000).
Motoshima H., Inagaki K., Kumasaka T., Furuichi M., Inoue H., Tamura T., Esaki N., Soda K., Tanaka N.,Yamamoto M., and Tanaka H.: “Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine
BL45XUγ-lyase from Pseudomonas putida”, J. Biochem. 128, 349-354 (2000).
Hishiki T., Shimada H., Nagano S., Egawa T., Kanamori Y., Makino R., Park S.-Y., Adachi S., Shiro Y.,
and Ishimura Y.: “X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome
P450cam: Roles of Thr252 and water in the active center”, J. Biochem. 128, 965-974 (2000).
BL44B2
Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H., Adachi S., Shoun H., andShiro Y.: “Proton delivery in NO reduction by fungal nitric-oxide reductase”, J. Biol. Chem. 275,4816-4826 (2000).
BL44B2
Hirao I., Madin K., Endo Y., Yokoyama S., and Ellington A. D.: “RNA aptamers that bind to and inhibit
the ribosome-inactivating protein, pepocin”, J. Biol. Chem. 275, 4943-4948 (2000).
Mitsuhashi S., Mizushima T., Yamashita E., Yamamoto M., Kumasaka T., Moriyama H., Ueki T., Miyachi
S., and Tsukihara T.: “X-ray structure of β-carbonic anhydrase from the red alga, Prophyridium
purpureum, reveals a novel catalytic site for CO2 hydration”, J. Biol. Chem. 275, 5521-5526 (2000).
BL45XU
Yamagata A., Masui R., Kato R., Nakagawa N., Ozaki H., Sawai H., Kuramitsu S., and Fukuyama K.:“Interaction of UvrA and UvrB proteins with a fluorescent single-stranded DNA”, J. Biol. Chem. 275,13235-13242 (2000).
Ishijima J., Nakai T., Kawaguchi S., Hirotsu K., and Kuramitsu S.: “Free energy requirement for domain
movement of an enzyme”, J. Biol. Chem. 275, 18939-18945 (2000).
Elena P., Miyano M., Kanaoka Y., Urade Y., and Hayaishi O.: “Structural basis of hematopoietic
prostaglandin D synthase activity elucidated by site-directed mutagenesis”, J. Biol. Chem. 275,31239-31244 (2000).

Kim I., Muto Y., Watanabe S., Kitamura A., Futamura Y., Yokoyama S., Hosono K., Kawai G., Takaku H.,Domae N., Takio K., Sakamoto H., and Shimura Y.: “Interactions of a didomain fragment of theDrosophila sex-lethal protein with single-stranded uridine-rich origoribonucleotides derived from thetransformer and Sex-lethal messenger RNA precursors: NMR with residue-selective [5-2H]uridinesubstitutions”, J. Biomol. NMR 17, 153-165 (2000).
Lee D.-S.: “Dibutyl phthalate, an α-glucosidase inhibitor from Streptomyces melanosporofaciens”, J.
Biosci. Bioeng. 89, 271-273 (2000).
Lee D-S. and Lee S.-H.: “Biological activity of dihydrotanshinone I: Effect on apoptosis”, J. Biosci.
Bioeng. 89, 292-293 (2000).
Kitano K., Sasaki R., Nogi T., Fukami T. A., Nakagawa A., Miki K., and Tanaka I.: “Utilization ofmicrogravity to improve the crystal quality of biologically important proteins: Chaperonin-60, GrpE,
B-subunit of V-type ATPase, and MIF”, J. Cryst. Growth 210, 819-823 (2000).
Hai H., Miura T., Kobayashi T., Maéda Y., and Miki M.: “Conformational changes of thetroponin-tropomyosin complex on F-actin observed by fluorescence resonance energy transfer
measurements”, J. Fluoresc. 10, 193-201 (2000).
Kato M., Yano K., Matsuo F., Saito H., Katagiri T., Kurumizaka H., Yoshimoto M., Kasumi F., AkiyamaF., Sakamoto G., Nagawa H., Nakamura Y., and Miki Y.: “Identification of Rad51 alteration in patientswith bilateral breast cancer”, J. Hum. Genet. 45, 133-137 (2000).
Piersma S. R., Nojiri M., Tsujimura M., Noguchi T., Odaka M., Yohda M., Inoue Y., and Endo I.:“Arginine 56 mutation in the β subunit of nitrile hydratase: Importance of hydrogen bonding to thenon-heme iron center”, J. Inorg. Biochem. 80, 283-288 (2000).
Shimizu H., Park S.-Y., Lee D.-S., Shoun H., and Shiro Y.: “Crystal structures of cytochrome P450nor
and its mutants (Ser286→Val, Thr) in the ferric resting state at cryogenic temperature: A comparativeanalysis with monooxygenase cytochrome P450s”, J. Inorg. Biochem. 81, 191-205 (2000).
BL44B2
Obayashi E., Shimizu H., Park S.-Y., Shoun H., and Shiro Y.: “Mutation effects of a conserved threonine(Thr243) of cytochrome P450nor on its structure and function”, J. Inorg. Biochem. 82, 103-111 (2000).
BL44B2
Kawano Y., Kumagai T., Muta K., Matoba Y., Davis J., and Sugiyama M.: “The 1.5Å crystal structure ofa bleomycin resistance determinant from bleomycin-producing Streptomycin vertucullus”, J. Mol. Biol.
295, 915-925 (2000).
Matuura Y., Stewart M., Kawamoto M., Kamiya N., Saeki K., Yasunaga T., and Wakabayashi T.:“Structure basis for the higher Ca2+-activatin of the regulated actin-activated myosin ATPase observedwith Dictyostelium/Tetrahymena actin chimeras”, J. Mol. Biol. 296, 579-595 (2000).
Miyatake H., Mukai M., Park S.-Y., Adachi S., Tamura K., Nakamura H., Nakamura K., Tsuchiya T.,
Iizuka T., and Shiro Y.: “Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti:

Crystallographic, mutagenesis and resonance Raman spectroscopic studies”, J. Mol. Biol. 301, 415-431(2000).
BL44B2Lee S. J., Imamoto N., Sakai H., Nakagawa A., Kose S., Koike M., Yamamoto M., Kumasaka T., Yoneda
Y., and Tsukihara T.: “The adoption of a twisted structure of importin-β is essential for the protein-protein
interaction required for nuclear transport”, J. Mol. Biol. 302, 251-264 (2000).
BL45XU
Hasegawa K., Ono T., and Noguchi T.: “Vibrational spectra and ab initio DFT calculations of
4-methylimidazole and its different protonation forms: Infrared and Raman markers of the protonation
state of a histidine side chain”, J. Phys. Chem. B 104, 4253-4265 (2000).
Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T., Nakanishi S., Jingami H., andMorikawa K.: “Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor”,
Nature 407, 971-977 (2000).
BL45XU
Inoue M., Muto Y., Sakamoto H., and Yokoyama S.: “NMR studies on functional structures of theAU-rich element-binding domains of Hu antigen C”, Nucleic Acids Res. 28, 1743-1750 (2000).
Sasaki Y. C., Suzuki Y., Yagi N., Adachi S., Ishibashi M., Suda H., Toyota K., and Yanagihara M.:“Tracking of individual nanocrystals using diffracted X-rays”, Phys. Rev. E 62, 3843-3847 (2000).
Isogai Y., Ishii A., Ishida M., Mukai M., Ota M., Nishikawa K., and Iizuka T.: “Structural and functional
properties of designed globins”, Proc. Ind. Acad. Sci.: Chem. Sci. 112, 215-221 (2000).
Nogi T., Fathir I., Kobayashi M., Nozawa Y., and Miki K.: “Crystal structures of photosynthetic reaction
center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability andelectron transfer”, Proc. Natl. Acad. Sci. USA 97, 13561-13566 (2000).
Oka T., Yagi N., Fujisawa T., Kamikubo H., Tokunaga F., and Kataoka M.: “Time-resolved X-ray
diffraction reveals multiple conformations in the M-N transition of the bacteriorhodopsin photocycle”,
Proc. Natl. Acad. Sci. USA 97, 14278-14282 (2000).
BL45SAXS
Kuroda Y., Tani K., Matsuo Y., and Yokoyama S.: “Automated search of natively folded protein
fragments for high-throughput structure determination in structural genomics”, Protein Sci. 9, 2313-2321(2000).
Toyoda T., Tin O.F., Ito K., Fujiwara T., Kumasaka T., Yamamoto M., Garber M.B., and Nakamura Y.:“Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor
shows that a flexible hinge may act as a functional switch”, RNA 6, 1432-1444 (2000).
BL45XU
Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C.,
Okada T., Stenkamp R.E., Yamamoto M., and Miyano M.: “Crystal structure of rhodopsin: A G
protein-coupled receptor”, Science 289, 739-745 (2000).
BL45XU
Sugiura I., Nureki O., Ugaji Y., Kuwabara S., Shimada A., Tateno M., Lober B., Giegé R., Moras D.,
Yokoyama S., and Konno M.: “The 2.0Å Crystal structure of Thermus thermophilus methionyl-tRNA

synthetase reveals two RNA-binding modules present in other class I enzymes”, Structure 8, 197-208(2000).
Nakai T., Hasegawa T., Yamashita E., Yamamoto M., Kumasaka T., Ueki T., Nanba H., Ikenaka Y.,Takahashi S., Sato M., and Tsukihara T.: “Crystal structure of N-carbamyl-D-amino acid amidohydrolasewith a novel catalytic framework common to amidohydrolases”, Structure 8, 729-739 (2000). BL45XUIshikawa M., Hirao I., and Yokoyama S.: “Synthesis of 3-(2-deoxy-β-D-ribofuranosyl)pyridin-2-one and2-amino-6-(N, N-dimethylamino)-9-(2-deoxy-β-D-ribofuranosyl)purine derivatives for an unnatural basepair”, Tetrahedron Lett. 41, 3931-3934 (2000).