Crystallization and preliminary X-ray analysis of l-azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C
l‐Azetidine‐2‐carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring‐opening reaction that detoxifies l‐azetidine‐2‐carboxylate, an analogue of l‐proline. Recombinant l‐azetidine‐2‐carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnes...
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Published in | Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 7; pp. 801 - 804 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.06.2010
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Subjects | |
Online Access | Get full text |
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Summary: | l‐Azetidine‐2‐carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring‐opening reaction that detoxifies l‐azetidine‐2‐carboxylate, an analogue of l‐proline. Recombinant l‐azetidine‐2‐carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle‐shaped crystal belonged to space group P21, with unit‐cell parameters a = 35.6, b = 63.6, c = 54.7 Å, β = 105.5°. The crystal diffracted to a resolution of 1.38 Å. The calculated VM value was 2.2 Å3 Da−1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit. |
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Bibliography: | istex:8707FB969E13211F70179D2F8242CFDA7DFFEF60 ark:/67375/WNG-XVMC58B0-V ArticleID:AYF2BW5351 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309110017045 |