Slow cooling and temperature-controlled protein crystallography.
In cryocrystallography, rapid sample cooling is generally deemed essential to prevent solvent crystallization and associated sample damage. We show that by carefully and completely removing all external solvent, many protein crystals can be successfully cooled to T = 100 K at only 0.1 K/s without additional penetrating cryoprotectants. Slow cooling provides an alternative when flash cooling fails, and enables diffraction studies of protein structure and function at all temperatures between T = 300 K and T = 100 K.
Warkentin
Matthew
M
Physics Department, Cornell University, Ithaca, NY 14853, USA.
Thorne
Robert E
RE
D000818:Animals; D003080:Cold Temperature; D003460:Crystallization; D003461:Crystallography / Q000379:methods*; D044367:Phase Transition; D011506:Proteins / Q000737:chemistry*; D012997:Solvents; D013696:Temperature
D011506:Proteins; D012997:Solvents