Linked Life Data

15039579

Source:http://linkedlifedata.com/resource/pubmed/id/15039579

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2004-3-24
pubmed:abstractText
The catalytic domain of death-associated protein kinase (DAPK) has been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with PEG 8000 and magnesium acetate as precipitants. Complexes with the inhibitor staurosporine and its analogue BDB402 were also crystallized in the presence of PEG 400 and PEG 8000, respectively. Diffraction data were collected to 2.4 A for the native catalytic domain, to 2.9 A for the staurosporine complex and to 2.7 A for the BDB402 complex. All three crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 77.992, b = 109.909, c = 50.063 A for the catalytic domain, a = 78.911, b = 113.162, c = 50.658 A for the staurosporine complex and a = 77.337, b = 108.869, c = 50.186 A for the BDB402 complex. In both complexes the inhibitor molecule was clearly assigned in the difference Fourier map calculated on the basis of the phases obtained from the structure of the catalytic domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
764-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Crystallization and preliminary X-ray analysis of two inhibitor complexes of the catalytic domain of death-associated protein kinase.
pubmed:affiliation
Devision of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't