Protein crystal growth in microgravity-temperature induced large scale crystallization of insulin.
One of the major stumbling blocks that prevents rapid structure determination using x-ray crystallography is macromolecular crystal growth.  There are many examples where crystallization takes longer than structure determination.  In some cases, it is impossible to grow useful crystals on earth.  Recent experiments conducted in conjunction with NASA on various Space Shuttle missions have demonstrated that protein crystals often grow larger and display better internal molecular order than their earth-grown counterparts.  This paper reports results from three Shuttle flights using the Protein Crystallization Facility (PCF).  The PCF hardware produced large, high-quality insulin crystals by using a temperature change as the sole means to affect protein solubility and thus, crystallization.  The facility consists of cylinders/containers with volumes of 500, 200, 100, and 50 ml.  Data from the three Shuttle flights demonstrated that larger, higher resolution crystals (as evidenced by x-ray diffraction data) were obtained from the microgravity experiments when compared to earth-grown crystals.
Long
M M
MM
Center of Macromolecular Crystallography, University of Alabama at Birmingham 35294-0005, USA.
DeLucas
L J
LJ
Smith
C
C
Carson
M
M
Moore
K
K
Harrington
M D
MD
Pillion
D J
DJ
Bishop
S P
SP
Rosenblum
W M
WM
Naumann
R J
RJ
Chait
A
A
Prahl
J
J
Bugg
C E
CE
D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D004867:Equipment Design; D007328:Insulin / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013026:Space Flight / Q000295:instrumentation*; D013696:Temperature; D014893:Weightlessness
D007328:Insulin; D011506:Proteins