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

ABSTRACT: 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 Å resolution, as well as an anomalous data set to 1.84 Å resolution that was suitable for S-SAD phasing.

SUBMITTER: Thomsen M

PROVIDER: S-EPMC3855733 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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

Thomsen Maren M Skalden Lilly L Palm Gottfried J GJ Höhne Matthias M Bornscheuer Uwe T UT Hinrichs Winfried W

Acta crystallographica. Section F, Structural biology and crystallization communications 20131129 Pt 12

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 Å resolution, as well as an anomalous data set to 1.84 Å resolution that was suitable for S-SAD phasing. ...[more]

PMID: 24316843

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