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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1990-3-1
|
| pubmed:abstractText |
Bovine lens gamma IVa-crystallin crystallizes in space group C222(1) with cell dimensions a = 35.1, b = 46.2, c = 186.2 A, and contains one molecule in the asymmetric unit. The structure was determined at 3.0 A resolution using cross-rotation functions and R-factor searches with the bovine lens protein gamma II-crystallin as the model structure. The rotation function appears to be very sensitive to the resolution range and type of coefficient employed; the use of normalized structure-factor amplitudes gave the best results. The potential problem of a pseudo solution due to an internal pseudo-twofold axis was put to advantage by aligning this axis parallel to z. The results of the R-factor search were well defined. The molecular replacement solution was improved by rigid-body least-squares refinement, initially of the whole molecule, then for the two domains. The R factor at this stage was 39.4% at 2.3-10.0 A. The gamma IVa structure has an even higher internal symmetry than gamma II, since the two domains are related by a rotation around the pseudo-twofold axis of 178.7 degrees as compared with 176.2 degrees for gamma II.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0108-7681
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
44 ( Pt 2)
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
172-8
|
| pubmed:dateRevised |
2007-7-24
|
| pubmed:meshHeading | |
| pubmed:year |
1988
|
| pubmed:articleTitle |
The use of pseudosymmetry in the rotation function of gamma IVa-crystallin.
|
| pubmed:affiliation |
Department of Crystallography, Birkbeck College, London, England.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|