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- W1967413563 abstract "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." @default.
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- W1967413563 date "2003-11-27" @default.
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- W1967413563 title "<i>Acetobacter turbidans</i>α-amino acid ester hydrolase: merohedral twinning in<i>P</i>2<sub>1</sub>obscured by pseudo-translational NCS" @default.
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- W1967413563 doi "https://doi.org/10.1107/s0907444903020729" @default.
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