Crystallization and preliminary X-ray diffraction studies of the (R)-selective amine transaminase from Aspergillus fumigatus

被引：8

作者：

Thomsen, Maren ^{[1
]}

Skalden, Lilly ^{[1
]}

Palm, Gottfried J. ^{[1
]}

Hoehne, Matthias ^{[1
]}

Bornscheuer, Uwe T. ^{[1
]}

Hinrichs, Winfried ^{[1
]}

机构：

[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, D-17489 Greifswald, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

关键词：

CRYSTAL-STRUCTURES; AMINOTRANSFERASE; RECOGNITION; RESOLUTION; ENZYMES; MODEL;

D O I：

10.1107/S1744309113030923

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The (R)-selective amine transaminase from Aspergillus fumigatus was expressed in Escherichia coli and purified to homogeneity. Bright yellow crystals appeared while storing the concentrated solution in the refrigerator and belonged to space group C222(1). X-ray diffraction data were collected to 1.27 angstrom resolution, as well as an anomalous data set to 1.84 angstrom resolution that was suitable for S-SAD phasing.

引用

页码：1415 / 1417

页数：3

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