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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1991-5-6
|
| pubmed:abstractText |
Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100.4 A and alpha = beta = gamma = 81.2 degrees. The asymmetric unit contains either a dimeric enzyme molecule, or a monomer.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
218
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
269-70
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:1826331-Bisphosphoglycerate Mutase,
pubmed-meshheading:1826331-Cloning, Molecular,
pubmed-meshheading:1826331-Crystallization,
pubmed-meshheading:1826331-Erythrocytes,
pubmed-meshheading:1826331-Escherichia coli,
pubmed-meshheading:1826331-Gene Expression,
pubmed-meshheading:1826331-Humans,
pubmed-meshheading:1826331-X-Ray Diffraction
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase.
|
| pubmed:affiliation |
Laboratoire de Biologie Physicochimique, CNRS UA1131, Université Paris-Sud, Orsay, France.
|
| pubmed:publicationType |
Journal Article
|