ArticleActa crystallographica. Section F, Structural biology communications2016
Cryoannealing-induced space-group transition of crystals of the carbonic anhydrase psCA3.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Streamlining heterologous expression of top carbonic anhydrases in Escherichia coli: bioinformatic and experimental approaches.Microbial cell factories · 2024Article
- Binding of Glycerol to Human Galectin-7 Expands Stability and Modulates Its Functions.International journal of molecular sciences · 2022Article
- Dependence of phase transition uniformity on crystal sizes characterized using birefringence.Structural dynamics (Melville, N.Y.) · 2021Article
- Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker.International journal of molecular sciences · 2016Article
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Authors and funding
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Abstract
Cryoannealing has been demonstrated to improve the diffraction quality and resolution of crystals of the β-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 Å 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 Å 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.
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