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In situ data collection and structure refinement from microcapillary protein crystallization
Author(s) -
Yadav Maneesh K.,
Gerdts Cory J.,
Sanishvili Ruslan,
Smith Ward W.,
Roach L. Spencer,
Ismagilov Rustem F.,
Kuhn Peter,
Stevens Raymond C.
Publication year - 2005
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s002188980502649x
Subject(s) - in situ , protein crystallization , crystallization , resolution (logic) , thaumatin , diffraction , crystallography , materials science , scattering , chemistry , analytical chemistry (journal) , optics , chromatography , physics , computer science , organic chemistry , biochemistry , artificial intelligence , gene
In situ X‐ray data collection has the potential to eliminate the challenging task of mounting and cryocooling often fragile protein crystals, reducing a major bottleneck in the structure determination process. An apparatus used to grow protein crystals in capillaries and to compare the background X‐ray scattering of the components, including thin‐walled glass capillaries against Teflon, and various fluorocarbon oils against each other, is described. Using thaumatin as a test case at 1.8 Å resolution, this study demonstrates that high‐resolution electron density maps and refined models can be obtained from in situ diffraction of crystals grown in microcapillaries.