Source:http://linkedlifedata.com/resource/pubmed/id/11976500
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 5
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pubmed:dateCreated |
2002-4-26
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pubmed:abstractText |
Carbonic anhydrases catalyze the interconversion of carbon dioxide to bicarbonate. Human carbonic anhydrase isozyme III with a C-terminal hexahistidine tag was overexpressed in Eschericha coli, purified and crystallized. Diffraction data (93.4% completeness) were collected to 2.2 A resolution on an in-house R-AXIS IV++ image-plate system with Osmic mirrors and a Rigaku HU-H3R CU rotating-anode generator operating at 50 kV and 100 mA. A 60 degrees sweep of data were collected from a single crystal with a crystal-to-detector distance of 150 mm and a 0.5 degrees oscillation angle per frame using an exposure of 60 s per frame at 293 K. The crystals were shown to conform to the Laue hexagonal crystal system P6, with unit-cell parameters a = 44.7, c = 222.5 A and a scaling R(sym) of 0.087 for 11 962 unique reflections. Using the known crystal structure of the rat form of carbonic anhydrase isozyme III, a molecular-replacement model was built. This model was used for rotation and translation searches and uniquely defined the space group as P6(5). Rigid-body refinement of the model was used to generate an initial phased electron-density map with an R(work) of 31.17%.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
849-52
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11976500-Amino Acid Sequence,
pubmed-meshheading:11976500-Animals,
pubmed-meshheading:11976500-Carbonic Anhydrase II,
pubmed-meshheading:11976500-Carbonic Anhydrase III,
pubmed-meshheading:11976500-Crystallography, X-Ray,
pubmed-meshheading:11976500-Escherichia coli,
pubmed-meshheading:11976500-Humans,
pubmed-meshheading:11976500-Molecular Sequence Data,
pubmed-meshheading:11976500-Protein Conformation,
pubmed-meshheading:11976500-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
Crystallization and preliminary X-ray analysis of human carbonic anhydrase III.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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