5JJ8

Crystal Structure of the Beta Carbonic Anhydrase psCA3 isolated from Pseudomonas aeruginosa - alternate crystal packing form

Summary for 5JJ8

• Entry DOI: 10.2210/pdb5jj8/pdb
• Descriptor: Carbonic anhydrase, ZINC ION (3 entities in total)
• Functional Keywords: psca3, crystal packing, beta-carbonic anhydrase, lyase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 48631.95

Authors

Pinard, M.A.,Kurian, J.J.,Aggarwal, M.,Agbandje-McKenna, M.,McKenna, R. (deposition date: 2016-04-22, release date: 2016-07-06, Last modification date: 2023-09-27)

Primary citation

Pinard, M.A.,Kurian, J.J.,Aggarwal, M.,Agbandje-McKenna, M.,McKenna, R.
Cryoannealing-induced space-group transition of crystals of the carbonic anhydrase psCA3.
Acta Crystallogr.,Sect.F, 72:573-577, 2016

PubMed 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.

PubMed: 27380376
DOI: 10.1107/S2053230X16009286

Experimental method

X-RAY DIFFRACTION (2.585 Å)