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 fr om 0.1 M sodium acetate buffer, pH 4.6, and 2% PEG 20000, using macros eeding techniques. The crystals diffract X-rays to al least 2.0 Angstr om nominal resolution. They belong to space group C2 with unit cell di mensions a = 93.2 Angstrom, b = 93.1 Angstrom, c = 45.6 Angstrom, alph a = 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 pack ing density of the crystals, there is one monomer in the asymmetric un it, resulting in a calculated solvent content of 48.2%.