Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II

被引：4

作者：

Lamb, AL ^{[1
]}

Wang, XS

Napoli, JL

Newcomer, ME

机构：

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

[2] SUNY Buffalo, Sch Med & Biomed Sci, Dept Biochem, Buffalo, NY 14214 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444997014121

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

One enzyme which catalyzes the last step of the formation of the hormone retinoic acid from vitamin A (retinol) is retinal dehydrogenase type II (RalDH2). RalDH2, expressed in the Escherichia coli BL21(DE3) strain, was purified and crystallized using ammonium sulfate as a precipitant. These crystals belong to the space group P2(1)2(1)2(1) (a = 108, b = 150, c = 168 Angstrom, alpha = beta = gamma = 90 degrees).

引用

页码：639 / 642

页数：4

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