Linked Life Data

21045291

Source:http://linkedlifedata.com/resource/pubmed/id/21045291

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2010-11-3
pubmed:abstractText
The nucleoside triphosphate hydrolases that are produced by Neospora caninum (NcNTPase) and Toxoplasma gondii (TgNTPase-I) have a different physiological function from the ubiquitous ecto-ATPases. The recombinant enzymes were crystallized at 293?K using polyethylene glycol 3350 as a precipitant and X-ray diffraction data sets were collected for NcNTPase (to 2.8?Å resolution) and TgNTPase-I (to 3.1?Å resolution) at 100?K using synchrotron radiation. The crystals of NcNTPase and TgNTPase-I belonged to the orthorhombic space group I222 (unit-cell parameters a = 93.6, b = 140.8, c = 301.1?Å) and the monoclinic space group P2(1) (unit-cell parameters a = 87.1, b = 123.5, c = 120.2?Å, ? = 96.6°), respectively, with two NcNTPase (V(M) = 3.7?Å(3)?Da(-1)) and four TgNTPase-I (V(M) = 2.7?Å(3)?Da(-1)) molecules per asymmetric unit. SAD phasing trials using a data set (? = 0.97904?Å) collected from a crystal of selenomethionylated NcNTPase gave an initial electron-density map of sufficient quality to build a molecular model of NcNTPase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1445-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Crystallization and preliminary X-ray structural analysis of nucleoside triphosphate hydrolases from Neospora caninum and Toxoplasma gondii.
pubmed:affiliation
Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto 606-8585, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't