Crystallization and preliminary crystallographic data for oncomodulin
Oncomodulin, a parvalbumin-like calcium-binding protein isolated from rat tumours, has been crystallized from 33% polyethylene glycol 6000 at pH 5·2 in the presence of CaCl 2 and dithiothreitol. The crystals belong to the space group P2 12 12 1, with unit cell dimensions a = 39·59(1) A ̊ , b = 64·28...
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Veröffentlicht in: | Journal of molecular biology 1988-01, Vol.199 (2), p.393-394 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Oncomodulin, a parvalbumin-like calcium-binding protein isolated from rat tumours, has been crystallized from 33% polyethylene glycol 6000 at pH 5·2 in the presence of CaCl
2 and dithiothreitol. The crystals belong to the space group
P2
12
12
1, with unit cell dimensions
a = 39·59(1)
A
̊
, b = 64·28(2)
A
̊
and
c = 33·07(1)
A
̊
, and have one molecule of oncomodulin per asymmetric unit. Their solvent content is only 31% (
v
v
) and they are remarkably stable. Three complete sets of data, one to 1·85 Å resolution for the native protein and one to 2·0 Å for each of two heavy-atom derivatives, have been collected. A three-dimensional structure analysis is in progress. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1016/0022-2836(88)90324-5 |