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Successful protein cryocooling for powder diffraction
Author(s) -
Jenner Mark J.,
Wright Jonathan P.,
Margiolaki Irene,
Fitch Andrew N.
Publication year - 2007
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/s0021889806044943
Subject(s) - powder diffraction , microcrystalline , diffraction , tetragonal crystal system , x ray crystallography , synchrotron , materials science , crystallography , resolution (logic) , analytical chemistry (journal) , chemistry , optics , crystal structure , chromatography , physics , artificial intelligence , computer science
It is shown that samples of microcrystalline tetragonal chicken egg white lysozyme can be effectively cryoprotected for high‐resolution synchrotron X‐ray powder diffraction studies at 100 K. The survival of the powder in the beam is increased by a factor of around 30. Thus, a high‐quality powder diffraction pattern could be collected at 100 K, which attains a resolution of d min ≃ 2.6 Å, significantly better than the previous limit of ∼3.27 Å at room temperature, despite a smaller volume of sample. Systematic variations of the concentration and type of cryoprotectant agent show that the lattice microstrains that accompany cooling, and degrade the quality of the powder diffraction data by broadening the diffraction peaks, are caused by a collapse in the volume of the crystalline unit cell.