rdf:type |
|
lifeskim:mentions |
umls-concept:C0010423,
umls-concept:C0017262,
umls-concept:C0043309,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0282535,
umls-concept:C0439611,
umls-concept:C0936012,
umls-concept:C1427622,
umls-concept:C1998793,
umls-concept:C2911684
|
pubmed:issue |
Pt 4
|
pubmed:dateCreated |
2009-4-3
|
pubmed:abstractText |
The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K. A complete data set was collected to 2.5 A resolution at 110 K. The crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 A.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-11256992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-12186888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-15322546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-15467982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-16240161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-16453322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-17377524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-18054307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-18636121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-7531706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19342780-7664083
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1744-3091
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
361-3
|
pubmed:dateRevised |
2011-7-27
|
pubmed:meshHeading |
pubmed-meshheading:19342780-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:19342780-Amino Acid Sequence,
pubmed-meshheading:19342780-Chromatography, Gel,
pubmed-meshheading:19342780-Crystallization,
pubmed-meshheading:19342780-Crystallography, X-Ray,
pubmed-meshheading:19342780-Humans,
pubmed-meshheading:19342780-Light,
pubmed-meshheading:19342780-Molecular Sequence Data,
pubmed-meshheading:19342780-Recombinant Proteins,
pubmed-meshheading:19342780-Scattering, Radiation,
pubmed-meshheading:19342780-Sequence Alignment,
pubmed-meshheading:19342780-src Homology Domains
|
pubmed:year |
2009
|
pubmed:articleTitle |
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1.
|
pubmed:affiliation |
Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, People's Republic of China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|