Acetobacter turbidans α-amino acid ester hydrolase:: merohedral twinning in P21 obscured by pseudo-translational NCS

被引：20

作者：

Barends, TRM ^{[1
]}

Dijkstra, BW ^{[1
]}

机构：

[1] Univ Groningen, NL-9747 AG Groningen, Netherlands

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903020729

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure elucidation of the alpha-amino acid ester hydrolase from Acetobacter turbidans by molecular replacement is described. In the monoclinic crystal, the molecules are related by both rotational and pseudo-crystallographic translational NCS (non-crystallographic symmetry). Refinement of the structure converged at unacceptably high R factors. After re-evaluation of the data, it was found that the crystal was merohedrally twinned, with a high twinning fraction. It is shown that the pseudo-crystallographic NCS causes aberrant behaviour of conventional twinning indicators, which explains why the twinning was only realized at the refinement stage.

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页码：2237 / 2241

页数：5

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