Open AccessPreliminary X‐ray crystallographic analysis of α‐carbonic anhydrase from Thiomicrospira crunogena XCL‐2
Author(s) -
Díaz Torres Natalia,
González Guillermo,
Biswas Shyamasri,
Scott Kathleen M.,
McKenna Robert
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112031053
Subject(s) - crystallography , carbonic anhydrase , molecule , x ray crystallography , chemistry , carbonic anhydrase ii , molecular replacement , crystal structure , diffraction , biochemistry , enzyme , physics , organic chemistry , optics
Thiomicrospira crunogena XCL‐2 is a novel sulfur‐oxidizing chemolithoautotroph that plays a significant role in the sustainability of deep‐sea hydrothermal vent communities. This recently discovered gammaproteobacterium encodes and expresses four carbonic anhydrases (CAs) from three evolutionarily and structurally distinct CA families: an α‐CA, two β‐CAs and a γ‐CA. In order to characterize and elucidate the physiological roles of these CAs, X‐ray crystallographic structural studies have been initiated on the α‐CA. The α‐CA crystallized in space group C 2. The crystals diffracted to a maximum resolution of 2.6 Å, with unit‐cell parameters a = 127.1, b = 102.2, c = 105.0 Å, β = 127.3°, and a calculated Matthews coefficient of 2.04 Å 3 Da −1 with four identical protein molecules in the crystallographic asymmetric unit. A preliminary solution was determined by molecular replacement with the PHENIX AutoMR wizard, which had an initial TFZ score of 17.9. Refinement of the structure is currently in progress.