Protein crystals can be very difficult to grow. Even protein crystallographers are often unable

to produce crystals of the high quality that is required to determine the molecular structure

of many proteins. As part of NASA’s educational outreach activities, we have prepared a simple

‘recipe’ for growing protein crystals from Brazil nuts. Please let us know how your attempts at

growing these protein crystals turn out. You may contact us at: 

microgravitynews@msfc.nasa.gov

For more up-to-date information about NASA’s macromolecular crystallography program, see:

http://crystal.nasa.gov

Introduction

Many hours of scientific study and investigation are invested in growing protein crystals – crystalsthat, when nearly perfect in form, are very highly prized. The information they reveal about a

protein’s molecular structure makes them very sought after and important to science. Proteins, macromolecules involved in everyday functions of the body such as transporting oxygen and chemicals in

blood, forming major components of muscle and skin, and fighting disease, come in over 100,000

varieties. Active sites on molecules of proteins, when inappropriately triggered or absent, can cause

disease or an unwanted function. Scientists seek to locate those active sites so drug designers can

understand their function and then, in some cases, work to block them or render them inactive. For

example, the anti-inflammatory drug ibuprofen works on a specific protein, which is involved early in the

signaling process that tells your body that inflammation should occur. Blocking the active site on this

protein prevents or reduces the inflammation. 

Educational Brief

A NASA Recipe For Protein Crystallography

Educational Products

Educators 

and Students

Grades

9 - 12

EB-2000-10-183-MSFC

National Aeronautics and

Space Administration

1

Glucose Isomerase Crystals Lysozyme Crystals Excelsin Crystals

Note: all bold face words are referenced in the glossary in the back of this document.
Aprotein crystal is a three-dimensional array of molecules in

which every molecule or specific

group of molecules has the same

orientation and relationship to its

neighbors, as long as the chemical

environment of the solution surrounding the crystal remains the

same. When a protein crystal

forms, protein molecules or groups

of molecules align to produce a

repeating three-dimensional pattern

or array. The effect of bringing these molecules

together in this arrangement is called amplification.

Amplification can be thought of in this way: imagine a football stadium full of people. If only one

person stands up and yells, the sound produced is

not easily heard. But if everybody in the stadium

stands up, faces the same direction and yells at

the same time, that sound can be heard from a

great distance. A very similar thing happens during the analysis of a protein crystal. One protein

molecule, by itself, would produce a signal so

weak it would be undetectable. But if all the molecules in the crystal produced the same signal at

exactly the same time, then that signal would be

strong enough to be recorded and decoded. The

more closely oriented or aligned the molecules

making up the protein crystal are, the better the

signal, and the more accurate the molecular information. 

Unfortunately, protein molecules

are so small that humans can’t

see them individually, let alone find

a specific site on a molecule or

determine its molecular structure. If

one cell in the human body were the

size of a football stadium, one protein molecule would be approximately the size of a can of soda, and

one of the atoms making up that

protein molecule would be about the

size of the fine print on the can.

Comparative sizes of proteins and the atoms 

making up proteins

EB-2000-10-183-MSFC 2 A NASA Recipe For Protein Crystallography
A NASA Recipe For Protein Crystallography 3 EB-2000-10-183-MSFC

The first known published observation of thecrystallization of a protein was made by F.L.

Hunefeld in 1840 at Leipzig University in Germany.

While working with hemoglobin, Hunefeld obtained

flat, plate-like crystals of this protein when he

pressed the blood of an earthworm between two

slides of glass and allowed the blood to dry very

slowly. 

In 1851, Otto Funke, another German

researcher, published a series of articles in which

he described growing hemoglobin crystals by

successively diluting red blood cells with a solvent

such as pure water, alcohol or ether, followed by

slow evaporation of the solvent from the resulting

protein solution.

Early on, scientists grew crystals solely to purify

proteins. Not until the 1930’s did researchers begin

to focus their attention on crystals as a source of

structural information about protein molecules.

They turned to X-ray diffraction, a procedure in

which a pencil-lead-sized X-ray beam is directed

at a crystal. The X-ray beam is scattered by the

crystal, producing a signal that results in tiny pinpoints that can be recorded on film. Data from this

recorded X-ray diffraction pattern has a direct relationship to the protein’s molecular structure and can

be used to help reveal the structure of a molecule

of the particular protein under investigation. By the

1960’s, scientists were investigating the molecular

structures of an abundance of crystals grown by

biochemists. Further, there was a century-long

backlog of crystals to be investigated. By the

1970’s, however, the

X-ray crystallographers had become

more selective in

determining which

proteins needed to

be crystallized for

analysis, and production of the desired

crystals was no

longer meeting

demand. New

methods for growing higher-quality

crystals were needed. The inability of scientists to

produce crystals useable for successful analysis of

some proteins had become a bottleneck in the

process of determining the three-dimensional structures of the molecules of many important proteins.

Typically a protein crystal must be structurally well

ordered and from about 0.2 to 0.5 mm in size. With

a high water content, protein crystals are usually

quite fragile and somewhat difficult to handle.

Protein crystals can be described as "soft" in contrast to a "hard" salt crystal.

X-ray beam penetrates a 

protein crystal

Molecular structure of 

the heme ring in the 

hemoglobin molecule

History
During the 1970’s, Walter Littke, a space

research pioneer and professor of chemistry at

the University of Freiburg, Germany, was using a

common method of growing protein crystals: placing

a salt solution together with the protein solution.

When two such solutions come in contact, the salt

becomes associated with some of the water molecules in which the protein is dissolved. This causes

the protein molecules to move closer together and

to begin to crystallize. However, many of the crystals produced by this method are fragile, and small

or broken.

By 1980, Littke suspected the culprit in his

unusable crystals to be convection, or fluid flow, in

the solution surrounding the growing protein crystals. This phenomenon occurs in normal gravity,

also known on Earth as one-g. Convection takes

place during crystal growth in one-g as protein molecules move from the surrounding solution and

assemble in an orderly way to become a part of the

growing crystal lattice. As protein molecules in the

solution move toward a crystal and become a part

of the crystal, the solution bordering the crystal then

contains a lower protein concentration than the

remainder of the solution and, therefore, it has a

lower density. This less-dense solution tends to

rise, and the denser solution sinks under the influence of gravity, creating fluid flows or convection,

next to the crystal. These convective currents can

have a negative effect on the quality of the crystal

being formed, because they can alter the orientation and position of the protein molecules as they

become a part of the crystal lattice. This can cause

disorder in the lattice structure of the protein crystal.

These imperfections in the crystal lattice, in turn,

adversely affect X-ray diffraction analysis results, or

the clarity with which a crystallographer can "see"

the precise position each atom occupies in the

three-dimensional structure of the protein molecule.

Another adverse effect of gravity on growing

crystals is sedimentation. Crystals drift to the bottom of a drop of the solution when they have grown

to a mass larger than can be supported by suspension in the drop. When this happens, partially

formed crystals fall on top of one another and continue growing into each other. Since X-ray diffraction analysis requires single crystals, sedimentation

renders potentially high-quality crystals unusable for

data collection.

Scientists began to consider the idea that in a

microgravity environment, with reduced convection

and sedimentation, protein molecules would move

together more slowly, primarily by diffusion. It was

expected that higher quality crystals could be produced in the microgravity environment, such as that

of the orbiting Space Shuttle.

But just how do scientists grow a protein crystal

in microgravity (or on Earth, for that matter), and

what do they do with it once they have grown it?

Researchers begin with a protein solution that is

supersaturated. A protein solution is prepared by

dissolving the protein, also called the solute, in a

solvent. Proteins have a solubility, which is a

measure of the amount of the protein (solute) that

can be dissolved in a given solvent, under specific

conditions. Growing a crystal, however, requires

supersaturation, which is a less stable condition that

results when somewhat more than maximum

amount of protein that can be dissolved in a solvent

under nominal conditions is, in fact, dissolved in the

solvent.

EB-2000-10-183-MSFC 4 A NASA Recipe For Protein Crystallography

Enter Microgravity
5

Most scientists don’t know the precise solubilityof the protein they may be investigating. A

researcher tests many different solution conditions

by varying such parameters as protein concentration, salt concentration and pH, in order to find the

best conditions required to promote the formation of

usable protein crystals. Once the researcher has

defined an optimum range of solution conditions, he

or she usually uses one of two methods for actually

growing the crystal: vapor diffusion or liquid/liquid

diffusion. Both methods involve changing the conditions of a protein solution to supersaturate the

solution. In vapor diffusion, the crystallographer

places a drop of protein solution in a chamber that

also holds a solution called a precipitant solution,

typically a salt solution. The salt in the precipitant

solution is more concentrated than salt that is in the

protein solution. This causes water vapor to diffuse

through the air from the drop to the precipitant solution. As water is removed from the drop, the protein

becomes more concentrated, causing protein molecules to move closer together and nucleate. In liquid/liquid diffusion, the researcher diffuses a salt

solution or some other precipitant solution in one

compartment of a two-chamber vial into a protein

solution in the other compartment. As the salt concentration increases, some of the water from the

protein solution becomes associated with the salt,

effectively raising the concentration of the protein in

the solution. Under these conditions the protein

molecules come together and begin to crystallize.

To analyze a protein crystal, an X-ray crystallographer shines an X-ray beam through the crystal.

Unlike a single dental X-ray, which produces a

shadow image of a tooth, these X-ray images have

to be taken many times from different angles to produce a pattern from the scattered X-ray beam. This

pattern is a map of the intensity of the X-rays after

they diffract through the crystal. The X-rays actually

bounce off the electron clouds that form the outer

structure of each atom. A flawed crystal will yield a

blurred pattern; a well-ordered protein crystal will

yield a series of sharp, more distinct diffraction patterns. 

From these patterns, researchers build an

electron density map. With powerful computers

capable of performing complex mathematical calculations, scientists can use the electron density

patterns to determine the structure of the protein

and make computer-generated models of the

three-dimensional structure of a protein molecule.

The models allow researchers to improve

understanding of how the protein functions. In addition, the models allow scientists to look for receptor

sites and active areas that control a protein’s function and role in the progression of

diseases.

X-ray diffraction pattern from

a protein crystal

A NASA Recipe For Protein Crystallography EB-2000-10-183-MSFC

Blueprint for Growing a Crystal

Electron Density Map
EB-2000-10-183-MSFC 6 A NASA Recipe For Protein Crystallography

Microgravity has been the chosen environment

for dozens of fundamental science experiments growing macromolecular crystals. Since

NASA’s protein crystal growth program began, principal investigators and their research teams have

flown samples of a total of 185 different proteins,

RNA’s, DNA’s and viruses (as of August 1999). The

macromolecules these scientists have studied

range from insulin to lactate dehydrogenase ( a

major enzyme in energy production and an important muscle protein in all animals) to thaumatin (a

sweet tasting protein with potential as a sugar substitute.) Most of NASA’s protein crystal growth

experiments, conducted from 1985 to 1999, have

been flown on Space Shuttle missions. The

remainder were conducted on the Russian space

station Mir. 

Given the great strides NASA’s protein crystal

growth program has made since the first protein

crystal growth experiments were conducted in

microgravity, where is the field headed now? For

many, it is to the International Space Station (ISS).

The ISS will expand the opportunities for growing

crystals in microgravity, enabling continued

advances in understanding the fundamental science

of the crystal growth process. Crystals, which usually grow more slowly in microgravity, will have more

time to fully develop into usable specimens. Followup experiments, an important and common feature

of all ground-based research, will be more feasible

in space on the ISS. 

The International Space Station (ISS)

will provide a platform for long term

microgravity experiments

http://spaceflight.nasa.gov/station

Normal gravity vs. microgravity

grown insulin crystals

Earth (1g) Space (μg)

NASA Macromolecular Crystal Growth Results
7

Abilities Necessary to do Scientific Inquiry

Physical Science

Life Science

Science and Technology

Science in Personal and Social Perspectives

History and Nature of Science

1) Identify questions and concepts that guide

scientific investigations

2) Design and conduct scientific investigations

3) Use technology and mathematics to improve

investigations and communications

4) Formulate and revise scientific explanations

and models using logic and evidence

5) Recognize and analyze alternative explanations

and models

6) Communicate and defend a scientific argument

7) Understandings about scientific inquiry

1) Structure of atoms

2) Structure and properties of matter

3) Chemical reactions

4) Motions and forces

1) The cell

2) Molecular basis of heredity

3) Matter, energy, and organization in living

systems

4) Behavior of organisms

1) Abilities of technological design

2) Understandings about science and technology

1) Personal and community health

2) Science and technology in local, national, and

global challenges

1) Science as human endeavor

2) Nature of scientific knowledge

3) Historical perspectives

A NASA Recipe For Protein Crystallography EB-2000-10-183-MSFC

Connections to Academic Standards

This NASA Educational Brief supports the following National Academy of Sciences Science Content

Standards:

National Science Education Content Standards (Grades 9-12) supported by the NASA Recipe for

Protein Crystallography.
Isolation, Crystallization & Purification of

Excelsin From Brazil Nuts

Ground Brazil nuts can be extracted with 5% aqueous NaCl at 50 ̊ to 70 ̊ C, filtered, then dialyzed

against distilled water to obtain crystals. 

This activity takes approximately 60 minutes

(CAUTION: Glass wool should only be handled while wearing gloves.)

Key Words

Aqueous Dialysis Membrane (or tubing) Morphology

Clarify Centrifuge Pellet

Decant Opaque Dialyze

Filtrate Denature Supernatant

Materials

Funnel Styrofoam (for bottom of 500 ml beaker)

Water (distilled preferred) Table Salt (sodium chloride)

Brazil Nuts (raw, organically grown) Glass Rod 

Centrifuge Tubes Cheesecloth, Glass Wool, or Filter Paper

Dialysis Membrane (app. 20 cm in length) Pipette or Medicine Dropper

50 ml graduated cylinder Thermometer

500 ml and 150 ml beakers Heating Plate

Small clamp(s) Small Centrifuge (up to 3000rpm)(optional) 

Blender or Coffee Grinder Laboratory Balance

EB-2000-10-183-MSFC 8 A NASA Recipe For Protein Crystallography
A NASA Recipe For Protein Crystallography 9 EB-2000-10-183-MSFC

Methods

Oil

Nut Meats

Aqueous Protein

Solution

Pellet

I. Isolation of Excelsin

1) Record the mass of ~ 8 or 9 raw Brazil nuts

(preferably organically grown). Grind the nuts

to granular size. 1 nut has a mass of approximately 2.8 grams.

2) Prepare a 5% sodium chloride (NaCl) solution

by dissolving 10 grams of solid NaCl in 200

milliliters of distilled water. Measure 25 ml of

5% NaCl solution into a graduated cylinder

and then pour into a 150 ml beaker. Record

the volume of NaCl solution in the beaker.

(Reserve remaining 5% NaCl solution for making 1% NaCl solution in Part II.3.)

3) Create a water bath by placing a flat piece of

styrofoam (can be cut from the bottom of a styrofoam cup) into the bottom of a 500 ml

beaker. Pour approximately 50 ml of water into

the 500 ml beaker. Place the smaller 150 ml

beaker (that contains the NaCl solution) in the

larger 500 ml beaker (that contains the water).

Place the beaker assembly on the heating

plate and heat until the water is at 50 ̊C.

Measure the final temperature and record.

4) Add the ground nuts to the NaCl solution in the

150 ml beaker and stir with a glass rod to mix.

Continue heating the water bath to maintain

the temperature of the NaCl solution and

ground nut mixture at 50 ̊C to 70 ̊C for 20 minutes, stirring occasionally. Record the temperature at regular intervals. (Be careful not to stir

vigorously or to heat above the designated

temperature range because this may cause

the protein to denature or break down).

5) (Caution: Glass wool should only be handled when wearing gloves.) Place 1-2 layers

of glass wool (or 10 layers of cheesecloth or

filter paper) in a funnel and place over a

beaker. Pour the NaCl/nut mixture through

glass wool. Measure and record the volume

of filtrate. (Note: Filtrate should be opaque.)

6) Option 1 - For classrooms without a centrifuge: Skip steps 7-9 and go directly to the

Crystallization of Excelsin in Section II.
EB-2000-10-183-MSFC 10 A NASA Recipe For Protein Crystallography

7) Option 2 - For classrooms with a centrifuge:

Pour filtrate into two centrifuge tubes and weigh

to make sure tubes are of equal weight.

Record the mass of each centrifuge tube.

8) Centrifuge for 20 minutes at 3000 rpm.

Referring to the diagram from the previous

page, pipette off the oil (top layer) and discard.

Carefully push the pipette through the nut meat

layer into the aqueous layer and decant off the

aqueous portion (located above the pellet and

just below the oil). Discard the pellet and oil.

9) Centrifuge the supernatant to clarify the solution further. The supernatant should now be a

fairly clear brown or brownish-yellow solution.

Measure and record the volume of the extracted protein solution.

1) Soak the dialysis membrane (small molecular

weight, preferably below 100,000 MWCO

(molecular weight cut off)) in room temperature

water for 5 minutes or longer. Take the membrane out of the beaker and tie a knot in one

end. Refer to page 12 for procedures on the

handling of dialysis tubing.

2) Pour the extracted protein/filtrate solution from

step 5 or 8 above into the dialysis

membrane/tubing and tie the other end of the

membrane.

3) Prepare 500 ml of 1% NaCl solution by combining 100 ml of 5% NaCl solution and 400 ml of

distilled water. Dialyze the protein solution

against the 500 ml of 1% NaCl solution. The

volume of the 1% NaCl solution should be at

least three times the measured volume of the

extracted solution. Record the volume of protein filtrate/solution and 1% NaCl solution.

Crystals should appear 4 - 10 hours later (They

will appear as white powder in the bottom of

the bag). If crystals do not appear in the 1%

NaCl solution, lower the NaCl concentration to

0%.

4) When the white powder appears, view it under

a microscope while the solution is still in the

bag.

1) Cut one end of the dialysis membrane bag

and decant the solution off of the crystals.

2) Add just enough 5% NaCl solution (1-3 ml) to

get the crystals to go back into solution. Either

retie the bag or seal the open end with a clamp.

Place the bag into a fresh solution of 1% NaCl

and allow to dialyze overnight, or until crystals

appear. Record information about crystals: size,

number, and morphology.

3) By repeating this dialysis process, a protein

can usually be rendered essentially pure. To

obtain larger crystals, slowly decrease the concentration of NaCl in solution. For example,

instead of going directly to 1% NaCl, start with

4.5% and decrease in increments of 0.5%. 

III. Recrystalization and Purification of Excelsin

II. Crystallization of Excelsin
Lab Record

Step Procedure Record

I(1) Brazil nut mass (grams) g

I(2) Volume of NaCl solution (ml) ml

I(3) Temperature of water bath ( ̊C)  ̊C

I(4) Temperature of NaCl/nut solution ( ̊C) – 1st recording  ̊C

I(4) Temperature of NaCl/nut solution ( ̊C) – 2nd recording  ̊C

I(4) Temperature of NaCl/nut solution ( ̊C) – 3rd recording  ̊C

I(4) Temperature of NaCl/nut solution ( ̊C) – 4th recording  ̊C

I(4) Temperature of NaCl/nut solution ( ̊C) – 5th recording  ̊C

I(5) Volume of protein filtrate (ml) ml

I(6) Centrifuge tube #1 mass g

I(6) Centrifuge tube #2 mass mg

I(8) Volume of extracted protein solution (ml) ml

II(3) Volume of protein filtrate (ml) ml

II(3) Volume of 1% NaCl solution (ml) ml

II(3) Volume of 0% NaCl solution (ml) (if required) ml

III(2) Volume of 5% NaCl solution added to bag (ml) ml

III(2) Volume of 1% NaCl solution added for dialysis (ml) ml

III(3) Volume of 5% NaCl solution added to bag (ml) ml

III(3) Volume of 1% NaCl solution added for dialysis (ml) ml

Record the size, number and morphology of the final Excelsin crystals produced.

Crystal Morphology (check which box applies) Number Size

Excelsin Oily mm

Spherical mm

Platelike mm

Hexagonal mm

Needles mm

Other mm

A NASA Recipe For Protein Crystallography 11 EB-2000-10-183-MSFC
EB-2000-10-183-MSFC 12 A NASA Recipe For Protein Crystallography

PROCEDURES FOR HANDLING 

DIALYSIS TUBING

1) Soak the dialysis tubing in a beaker of distilled

water.

2) Tie the dialysis tubing making sure to tie the

knot from the top end toward the knot, ensuring

that the area to contain the protein solution is

not touched or handled. Touching the tubing

may increase the pore size of the tubing and

result in loss of protein.

3) Pour the protein solution into the dialysis tubing.

4) Tie the remaining open end of the tubing, leaving a small air pocket so the bag will float.

5) Place the dialysis bag in the NaCl solution (see

Lab Method step II.3.)

1 2 3

4 5
A NASA Recipe For Protein Crystallography 13 EB-2000-10-183-MSFC

GLOSSARY

Active site the portion of a molecule that binds with a substrate molecule

Aqueous relating to, similar to, containing, or dissolved in water; watery

Clarify to make clear by removing impurities or solid matter

Concentration a measurement of the amount of solute that is dissolved in a given quantity of solvent

Convection heat transfer in a gas or liquid by the circulation of currents from one region to another

Decant to pour off gently 

Denature to alter the structure of (a protein), as with heat, alkali, or acid, so that some of its 

original properties, especially its biological activity, are diminished or eliminated 

Density the ratio of the mass of an object to its volume

Dialysis/Dialyze the transfer of dissolved solids (solute) across a semipermeable membrane, which 

permits or hinders diffusion of molecules according to their size

Dialysis membrane a semipermeable casing used to dialyze a solution

(tubing)

Diffusion the spontaneous intermingling of molecules as a result of random thermal motion

Electron density map a graphical representation of the volume of space that an electron is most likely to

occupy; the smaller the volume of space occupied, the higher the electron density

Filtrate the liquid passing through the filter during filtration

Gravity the natural force of attraction of objects to each other due to their masses

Hemoglobin an iron-containing protein in red blood cells that carries oxygen from the lungs to the

rest of the body

Liquid/liquid diffusion the diffusion of a precipitant solution into a protein solution across their common

liquid/liquid interface

Macromolecule a very large molecule, such as a polymer or protein, consisting of many smaller 

structural units linked together

Microgravity an environment in which the apparent weight of a system is small compared to its

actual weight (due to gravity)

Molecular weight the sum of the weight of all the atoms in a molecule, also called 

formula weight
EB-2000-10-183-MSFC 14 A NASA Recipe For Protein Crystallography

Morphology the shape of a crystal

Nucleate to gather, as about a nucleus or center 

Opaque impenetrable by light; neither transparent nor translucent

Pellet a small, solid or densely packed mass 

pH a measure of the acidity or alkalinity of a solution, numerically equal to 7 for neutral

solutions, increasing with increasing alkalinity and decreasing with increasing acidity;

the pH scale commonly in use ranges from 0 to 14

Precipitant solution a solution which causes the formation of a precipitate

Precipitant a solid or solid phase separated from a solution

Protein any of a group of complex organic macromolecules composed of one or more chains

of amino acids; proteins are fundamental components of all living cells and include

many substances, such as enzymes, hormones, and antibodies, that are necessary for

the proper functioning of an organism

Receptor site a region, often the exposed part of a membrane protein, that binds a substance but

does not catalyze a reaction in the chemical it binds

Sediment the material that settles to the bottom of a liquid

Sedimentation the settling of materials to the bottom of a liquid; this settling is due to gravity

Solute the dissolved substance in a solution; in salt water, salt is the solute

Solution a homogeneous or uniform mixture of two or more substances

Solvent a substance used to dissolve a solute to form a solution; in salt water, water is the 

solvent

Supernatant the clear fluid floating above a sediment or precipitate

Supersaturated the state of a solution when it contains more solute (dissolved substance) than it can

theoretically hold

Vapor diffusion a process of diffusion in which a drop of protein solution is suspended above a precipitant and sealed from the air, resulting in equilibration through the vapor phase

X-ray diffraction the scattering of x-ray beams by crystal atoms, producing a diffraction pattern that

yields information about the structure of the crystal
A NASA Recipe For Protein Crystallography 15 EB-2000-10-183-MSFC

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EB-2000-10-183-MSFC 16 A NASA Recipe For Protein Crystallography

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A NASA Recipe For Protein Crystallography 17 EB-2000-10-183-MSFC

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Fax: (661) 948-7068

http://www.dfrc.nasa.gov/trc/

NASA JPL Educator Resource Center 

Village at Indian Hill 

1460 East Holt Avenue, Suite 20 

NASA Jet Propulsion Laboratory 

Pomona, CA 91767 

Phone: (909) 397-4420

Fax: (909) 397-4470

http://learn.jpl.nasa.gov

Arizona and

Southern California

Virginia and

Maryland’s Eastern

Shores

Mississippi

NASA Educator Resource Center

NASA Stennis Space Center 

Building 1200 

Stennis Space Center, MS 39529-6000 

Phone: (228) 688-3220 

FAX: (228) 688-2824 

http://education.scc.nasa.gov/htmls/trc/trc.htm 

Regional Educator Resource Centers offer more educators access to NASAeducational materials. NASA

has formed partnerships with universities, museums, and other educational institutions to serve as

regional ERCs in many states. A complete list of regional ERCs is available through CORE, or electronically via NASA Spacelink at http://spacelink.nasa.gov/ercn/ 

NASA's Education Home Page serves as a cyber-gateway to information regarding educational

programs and services offered by NASA for the American education community. This high-level

directory of information provides specific details and points of contact for all of NASA's educational

efforts, Field Center offices, and points of presence within each state. Visit this resource at the following address: http://education.nasa.gov

The Jet Propulsion

Laboratory (JPL)

serves inquiries related

to space and planetary

exploration and other

JPL activities.
EB-2000-10-183-MSFC 18 A NASA Recipe For Protein Crystallography

NASA Spacelink is one of NASA's electronicresources specifically developed for the educational community. Spacelink is a "virtual library"

in which local files and hundreds of NASA World

Wide Web links are arranged in a manner familiar

to educators. Using the Spacelink search engine,

educators can search this virtual library to find

information regardless of its location within NASA.

Special events, missions, and intriguing NASA

websites are featured in Spacelink's "Hot Topics"

and "Cool Picks" areas. Spacelink may be

accessed at: http://spacelink.nasa.gov 

NASA Spacelink is the official home to electronic

versions of NASA's Educational Products. A

complete listing of NASA Educational Products

can be found at the following address:

http://spacelink.nasa.gov/products 

NASA Television (NTV) features Space

Shuttle mission coverage, live special events,

interactive educational live shows, electronic field

trips, aviation and space news, and historical

NASA footage. Programming has a 3-hour block

— Video (News) File, NASA Gallery, and

Education File — beginning at noon Eastern and

repeated five more times throughout the day. Live

feeds preempt regularly scheduled programming. 

Check the Internet for program listings at:

http://www.nasa.gov/ntv 

For more information on NTV, contact: 

NASA TV 

NASA Headquarters 

Code P-2 

Washington, DC 20546-0001 

Phone (202) 358-3572 

NTV Weekday Programming Schedules 

(Eastern Times) 

Video File NASA Gallery Education File 

12-1 p.m. 1-2 p.m. 2-3 p.m. 

3-4 p.m. 4-5 p.m. 5-6 p.m. 

6-7 p.m. 7-8 p.m. 8-9 p.m. 

9-10 p.m. 10-11 p.m. 11-12 p.m. 

How to Access Information on NASA's

Education Program, Materials, and Services

EP-1999-06-345-HQ. 

This brochure serves as a guide to accessing a

variety of NASA materials and services for educators. Copies are available through the ERC network, or electronically via NASA Spacelink.

Spacelink & NASA Television

Online Evaluation

Please take a moment to evaluate this product at

http://ehb2.gsfc.nasa.gov/edcats/educational_brief

Your evaluation and suggestions are vital to continually

improving NASA educational materials.