Linked Life Data

15677718

Source:http://linkedlifedata.com/resource/pubmed/id/15677718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-2-9
pubmed:abstractText
In the Joint Center for Structural Genomics, one-dimensional (1D) 1H NMR spectroscopy is routinely used to characterize the folded state of protein targets and, thus, serves to guide subsequent crystallization efforts and to identify proteins for NMR structure determination. Here, we describe 1D 1H NMR screening of a group of 79 mouse homologue proteins, which correlates the NMR data with the outcome of subsequent crystallization experiments and crystallographic structure determination. Based on the 1D 1H NMR spectra, the proteins are classified into four groups, "A" to "D." A-type proteins are candidates for structure determination by NMR or crystallography; "B"-type are earmarked for crystallography; "C" indicates folded globular proteins with broadened line shapes; and "D" are nonglobular, "unfolded" polypeptides. The results obtained from coarse- and fine-screen crystallization trials imply that only A- and B-type proteins should be used for extensive crystallization trials in the future, with C and D proteins subjected only to coarse-screen crystallization trials. Of the presently studied 79 soluble protein targets, 63% yielded A- or B-quality 1D 1H NMR spectra. Although similar yields of crystallization hits were obtained for all four groups, A to D, crystals from A- and B-type proteins diffracted on average to significantly higher resolution than crystals produced from C- or D-type proteins. Furthermore, the output of refined crystal structures from this test set of proteins was 4-fold higher for A- and B-type than for C- and D-type proteins.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-10395471, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-11017201, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-11104003, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-11467927, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-11854485, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-12193646, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-12547425, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-12777766, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-12836706, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-15125680, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-15263836, http://linkedlifedata.com/resource/pubmed/commentcorrection/15677718-6055984
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1901-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.
pubmed:affiliation
Department of Molecular Biology and Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't