Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp alkalophilus



: Moser M, Muller R, Battchikova N, Koivulehto M, Korpela T, Jansonius JN

Publisher: WILEY-BLACKWELL

: 1996

: Protein Science

: PROTEIN SCIENCE

: PROTEIN SCI

: 5

: 7

: 1426

: 1428

: 3

: 0961-8368

DOI: https://doi.org/10.1002/pro.5560050721


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 al least 2.0 Angstrom nominal resolution. They belong to space group C2 with unit cell dimensions a = 93.2 Angstrom, b = 93.1 Angstrom, c = 45.6 Angstrom, alpha = 90.0 degrees, beta = 106.8 degrees, gamma = 90.0 degrees. A native data set to 2.3 Angstrom 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%.



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