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Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercurythiosalicylate.

作者信息

Pakhomova S, Luz J G, Kobayashi M, Mellman D, Buck J, Newcomer M E

机构信息

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1641-3. doi: 10.1107/s0907444900012671.

DOI:10.1107/s0907444900012671
PMID:11092933
Abstract

Retinol dehydratase is a sulfotransferase which is presumed to catalyze the dehydration of its substrate via a transient retinyl sulfate intermediate. Crystals (space group P2(1), unit-cell parameters a = 82.05, b = 66.61, c = 84.90 A, beta = 111.29 degrees ) are significantly improved by covalent modification of the protein with ethylmercury.

摘要

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