Source:http://linkedlifedata.com/resource/pubmed/id/11679748
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 11
|
| pubmed:dateCreated |
2001-10-26
|
| pubmed:abstractText |
The monomeric 3'-5' helicase RecG from the thermophilic bacterium Thermotoga maritima has been crystallized in complex with a three-way DNA junction, the preferred physiological substrate. The crystals were obtained by hanging-drop vapour diffusion. The crystals belong to space group C2, with unit-cell parameters a = 133.7, b = 144.6, c = 84.0 A, beta = 113.8 degrees. Native data to a resolution of 3.25 A were collected from crystals flash-cooled to 100 K.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0907-4449
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
57
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1695-6
|
| pubmed:dateRevised |
2007-7-24
|
| pubmed:meshHeading |
pubmed-meshheading:11679748-Bacterial Proteins,
pubmed-meshheading:11679748-Crystallization,
pubmed-meshheading:11679748-Crystallography, X-Ray,
pubmed-meshheading:11679748-DNA,
pubmed-meshheading:11679748-Escherichia coli Proteins,
pubmed-meshheading:11679748-Nucleic Acid Conformation,
pubmed-meshheading:11679748-Protein Conformation,
pubmed-meshheading:11679748-Thermotoga maritima
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray analysis of RecG, a replication-fork reversal helicase from Thermotoga maritima complexed with a three-way DNA junction.
|
| pubmed:affiliation |
Imperial Cancer Research Fund, Clare Hall Laboratories, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, England.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|