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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1982-4-20
|
| pubmed:abstractText |
X-ray diffraction data to 2.4-A resolution have been collected for native monoclinic crystals of the MoFe protein of nitrogenase from Clostridium pasteurianum. The MoFe protein is an alpha 2 beta 2 tetramer of 220,000 molecular weight with 1 molecule in the crystallographic asymmetric unit. A 6-A resolution rotation function shows the orientation of the crystallographic diad and pseudo mutually perpendicular diads representing 2-fold relationships between alpha and beta chains. Hence, at least at low resolution, there exists structural homology between these two polypeptide chains.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
257
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1221-3
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1982
|
| pubmed:articleTitle |
Molecular symmetry of the MoFe protein of nitrogenase. Structural homology/nitrogen fixation/x-ray crystallography.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|