Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus.
Recombinant phosphoserine aminotransferase (EC 2.6.1.52) from Bacillus circulans subsp. alkalophilus was crystallized at room temperature from 0.1 M sodium acetate buffer, pH 4.6, and 2% PEG 20000, using macroseeding techniques. The crystals diffract X-rays to at least 2.0 A nominal resolution. They belong to space group C2 with unit cell dimensions a = 93.2 A, b = 93.1 A, c = 45.6 A, alpha = 90.0 degrees, beta = 106.8 degrees, gamma = 90.0 degrees. A native data set to 2.3 A has been collected. Assuming an average packing density of the crystals, there is one monomer in the asymmetric unit, resulting in a calculated solvent content of 48.2%.
Moser
M
M
Department of Structural Biology, Biozentrum, University of Basel, Switzerland.
Müller
R
R
Battchikova
N
N
Koivulehto
M
M
Korpela
T
T
Jansonius
J N
JN
D001407:Bacillus / Q000201:enzymology*; D018360:Crystallography, X-Ray; D011994:Recombinant Proteins / Q000737:chemistry; D000637:Transaminases / Q000737:chemistry*
D011994:Recombinant Proteins; D000637:Transaminases; C022393:phosphoserine aminotransferase