Open AccessCrystallization and preliminary X‐ray diffraction studies of the ( R )‐selective amine transaminase from Aspergillus fumigatus
Author(s) -
Thomsen Maren,
Skalden Lilly,
Palm Gottfried J.,
Höhne Matthias,
Bornscheuer Uwe T.,
Hinrichs Winfried
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113030923
Subject(s) - aspergillus fumigatus , crystallization , transaminase , amine gas treating , aspergillus , chemistry , microbiology and biotechnology , biochemistry , biology , organic chemistry , enzyme
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 C 222 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.