Michael Braukus

Headquarters, Washington D.C.

September 23, 1993
(Phone: 202/358-1979)
EMBARGOED UNTIL NOON EDT

David B. Drachlis
Marshall Space Flight Center, Huntsville, Ala.
(Phone: 205/544-0034)

RELEASE: 93-166

PROTEIN CRYSTAL GROWTH RESEARCH TAKES STEP TOWARD NEW

DRUGS

Results from a Spacelab crystal growth experiment flown

aboard the Space Shuttle last summer have brought researchers a
step closer to understanding the molecular structure of proteins
which will aid scientists in developing more effective
disease-fighting, anti-parasitic drugs.

During the first United States Microgravity Laboratory

(USML-1) mission, Shuttle flight STS-50, crystals of Malic Enzyme
were produced that showed a dramatic improvement in resolution
over Earth-grown crystals.

"The USML-1 crystals were of such high quality that they make
it possible for researchers to determine the structure of this
important protein," said Dr. Lawrence DeLucas of the Center for
Macromolecular Crystallography at the University of Alabama in
Birmingham. DeLucas flew as a payload specialist on USML-1 and is
a principal investigator on many of the protein crystal growth
experiments.

This success follows 2 years and several hundred ground-based

crystallization trials, during which researchers were unable to
produce any crystals of high enough quality to allow determination
of this protein's structure.
 "On USML-1, using experiment hardware specifically designed
for the mission, we learned how to grow the high quality Malic
Enzyme crystals," explained DeLucas. "Then on Shuttle mission
STS-57 in June of this year, we produced additional crystals of
comparable quality. Now, we just need a few more flights to
accumulate enough of these superior crystals to complete the
process of structure identification."

Protein crystal growth experiments have flown on 18 Space

Shuttle missions since April 1985, producing a number of crystals
of a quality significantly superior to Earth-grown crystals.

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Researchers already have used superior space-grown crystals

to improve their knowledge of the structure of several proteins.
Space grown crystals have contributed to the refinement of
molecular structures of:

- Gamma Interferon, a protein important in anti-viral research and

for treatment of certain types of cancer;

- Human Serum Albumin, the most abundant protein in human blood

which is responsible for distribution of many different drugs,
including aspirin, to various body tissues;

- Elastase, a key protein known to cause the destruction of lung

tissue in patients suffering from emphysema; and

- Factor D, a protein important in inflammation and other immune

system responses.

Protein crystal growth experiments also have produced

superior quality crystals of:

- Isocitrate Lyase, a protein important for the development of

anti-fungal drugs;

- Canavalin, a protein isolated from edible plants whose structure

is of interest because the information can be used to genetically
engineer more nutritious plants; and

- Proline Isomerase, a protein important in and used as a drug for

diabetes.

"Although valuable new information was obtained from these

initial experiments, additional high quality crystals are needed
to obtain the final structures for many of these proteins,"
explained DeLucas. "Also, a constant supply of the crystals is
necessary for the drug design phase for those proteins associated
with various diseases."

"The experimental results gathered to date have conclusively

demonstrated that protein crystals of superior size and quality
can be produced in space," DeLucas pointed out. "And the results
clearly indicate the need for continued, constant and long-term
access to this unique microgravity environment."

During the record 14-day USML-1 mission, DeLucas and mission

specialists Dr. Bonnie Dunbar and Carl Meade investigated
techniques for improving the success rate for protein crystal
growth experiments and tested a variety of procedures being
considered for similar experiments to be performed aboard space
station.

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