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

✍ Scribed by Markus Moser; Rita Müller; Johan N. Jansonius; Natalia Battchikova; Marianne Koivulehto; Timo Korpela

Publisher
Cold Spring Harbor Laboratory Press
Year
1996
Tongue
English
Weight
321 KB
Volume
5
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

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 Å nominal resolution. They belong to space group C2 with unit cell dimensions a = 93.2 Å, b = 93.1 Å, c = 45.6Å, α = 90.0°, β = 106.8°, γ = 90.0°. A native data set to 2.3 Å 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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