Journal
JOURNAL OF APPLIED CRYSTALLOGRAPHY
Volume 39, Issue -, Pages 805-811Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0021889806037484
Keywords
-
Categories
Funding
- NIGMS NIH HHS [R01 GM065981, R01 GM065981-03] Funding Source: Medline
Ask authors/readers for more resources
When samples having volumes characteristic of protein crystals are plunge cooled in liquid nitrogen or propane, most cooling occurs in the cold gas layer above the liquid. By removing this cold gas layer, cooling rates for small samples and modest plunge velocities are increased to 1.5 x 10(4) K s(-1), with increases of a factor of 100 over current best practice possible with 10 mm samples. Glycerol concentrations required to eliminate water crystallization in protein-free aqueous mixtures drop from similar to 28% w/v to as low as 6% w/v. These results will allow many crystals to go from crystallization tray to liquid cryogen to X-ray beam without cryoprotectants. By reducing or eliminating the need for cryoprotectants in growth solutions, they may also simplify the search for crystallization conditions and for optimal screens. The results presented here resolve many puzzles, such as why plunge cooling in liquid nitrogen or propane has, until now, not yielded significantly better diffraction quality than gas-stream cooling.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available