COMMERCIAL PROTEIN CRYSTAL GROWTH-HIGH DENSITY (CPCG-H)
Research Area: Macromolecular Crystal Growth
Expedition(s): 2 and 4
Principal Investigator(s): ● Lawrence J. DeLucas, OD, PhD, University of Alabama at
Birmingham, Birmingham, Alabama
RESEARCH OBJECTIVES
Commercial Protein Crystal Growth - High Density (CPCG-H) tests hardware using a variety of
protein crystal growth methods. Researchers aim to determine the most appropriate type of
hardware for each experiment and which type of hardware could be permanently added to or
removed from International Space Station (ISS) facilities for future protein crystal experiments.
Protein crystal growth experiments aid the generation of computer models of carbohydrates,
nucleic acids and proteins, and further advance the progress of biotechnology. Understanding
these results can lead to advances in manufacturing and biological processes, both in medicine
and agriculture.
EARTH BENEFITS
Knowledge of precise 3-D molecular
structure is a key component in
biotechnology fields such as protein
engineering and pharmacology. In order
to obtain accurate data on the 3-D
structure of protein crystals or other
macromolecules, scientists employ a
process called X-ray crystallography.
Crystallographers construct computer
models that reveal the complex
structures of a protein molecule. In order
to generate an accurate computer model,
crystallographers must first crystallize the
protein and analyze the resulting crystals
by a process called X-ray diffraction.
Precise measurements of thousands of
diffracted intensities from each crystal
help scientists map the probable
positions of the atoms within each protein molecule. This complex process requires several
months to several years to complete.
The quality of structural information obtained from X-ray diffraction methods is directly
dependent on the degree of perfection of the crystals. Thus, the structures of many important
proteins remain a mystery simply because researchers are unable to obtain crystals of high
enough quality or large enough size. Generally, crystals must have dimensions of approximately
0.3 mm to 1.00 mm, and the protein molecules must be arranged in an orderly, repeating
pattern. Consequently, the growth of high quality macromolecular crystals for diffraction
Thermus flavus crystals of the 7bp helix B1 grown on the
International Space Station Expedition 2. Image provided by
Acta Crystallographica. Section D, Biological
Crystallography. Crystallization and Structure Analysis of
Thermus flavus 5S rRNA helix B.