|
type |
Journal Article |
authors |
Moser, M.; Muller, R.; Battchikova, N.; Koivulehto, M.; Korpela, T.; Jansonius, J. N. |
title |
Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus |
journal |
Protein Sci |
Activity |
2.6.1.52 |
Family |
2.6.1.52.a |
ui |
96416269 |
year |
(1996) |
volume |
5 |
number |
7 |
pages |
1426-8 |
| |
keywords |
Bacillus/*enzymology |
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 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%. |
last changed |
2020/02/20 18:07 |
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