Crystallization of retinol dehydratase from Spodoptera frugiperda:: improvement of crystal quality by modification by ethylmercury-thiosalicylate

被引：9

作者：

Pakhomova, S

Luz, JG

Kobayashi, M

Mellman, D

Buck, J

Newcomer, ME

机构：

[1] Vanderbilt Univ, Sch Med, Dept Biochem, Nashville, TN 37232 USA

[2] Cornell Univ, Coll Med, Dept Pharmacol, New York, NY 10021 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900012671

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom, beta = 111.29 degrees) are significantly improved by covalent modification of the protein with ethylmercury.

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页码：1641 / 1643

页数：3

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