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Publication Abstract from PubMed

Cryoannealing has been demonstrated to improve the diffraction quality and resolution of crystals of the beta-carbonic anhydrase psCA3 concomitant with a change in space group. After initial flash-cooling in a liquid-nitrogen cryostream an X-ray diffraction data set from a psCA3 crystal was indexed in space group P21212 and was scaled to 2.6 A resolution, but subsequent cryoannealing studies revealed induced protein rearrangements in the crystal contacts, which transformed the space group to I222, with a corresponding improvement of 0.7 A in resolution. Although the change in diffraction resolution was significant, only minor changes in the psCA3 structure, which retained its catalytic `open' conformation, were observed. These findings demonstrate that cryoannealing can be successfully utilized to induce higher diffraction-quality crystals while maintaining enzymatically relevant conformations and may be useful as an experimental tool for structural studies of other enzymes where the initial diffraction quality is poor.

Cryoannealing-induced space-group transition of crystals of the carbonic anhydrase psCA3.,Pinard MA, Kurian JJ, Aggarwal M, Agbandje-McKenna M, McKenna R Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):573-7. doi:, 10.1107/S2053230X16009286. Epub 2016 Jun 28. PMID:27380376^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.