Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
14
|
| pubmed:dateCreated |
1991-6-10
|
| pubmed:abstractText |
The mutT nucleoside triphosphatase, which prevents AT----CG transversions during DNA replication, has been crystallized from ammonium sulfate utilizing a novel technique involving vapor diffusion in capillaries. X-ray diffraction analysis has revealed that the crystals are monoclinic, space group P2(1), with cell constants a = 34.14, b = 72.54, c = 56.38, and beta = 98.90. The Vm value of 2.31 A3/Da is consistent with two molecules of enzyme per asymmetric unit. The crystals are reasonably stable in the x-ray beam, and a data set to 2.5 A resolution has been collected for native protein. There is evidence that the crystals diffract to at least 2.1 A.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
266
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
9055-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1851163-Crystallography,
pubmed-meshheading:1851163-Escherichia coli,
pubmed-meshheading:1851163-Nucleoside-Triphosphatase,
pubmed-meshheading:1851163-Phosphoric Monoester Hydrolases,
pubmed-meshheading:1851163-Protein Conformation,
pubmed-meshheading:1851163-Pyrophosphatases,
pubmed-meshheading:1851163-X-Ray Diffraction
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction studies on the mutT nucleoside triphosphate pyrophosphohydrolase of Escherichia coli.
|
| pubmed:affiliation |
McCollum-Pratt Institute, Baltimore, Maryland.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|