A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp alkalophilus
Tekijät: Moser M, Muller R, Battchikova N, Koivulehto M, Korpela T, Jansonius JN
Kustantaja: WILEY-BLACKWELL
Julkaisuvuosi: 1996
Lehti:: Protein Science
Tietokannassa oleva lehden nimi: PROTEIN SCIENCE
Lehden akronyymi: PROTEIN SCI
Vuosikerta: 5
Numero: 7
Aloitussivu: 1426
Lopetussivu: 1428
Sivujen määrä: 3
ISSN: 0961-8368
DOI: https://doi.org/10.1002/pro.5560050721
Tiivistelmä
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%.
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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