Structure determination of a lone alpha-helical antifreeze protein from winter flounder.
Identifieur interne : 002775 ( PubMed/Corpus ); précédent : 002774; suivant : 002776Structure determination of a lone alpha-helical antifreeze protein from winter flounder.
Auteurs : F. Sicheri ; D S YangSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 1996.
Abstract
The X-ray crystal structure of a lone alpha-helical antifreeze protein from winter flounder has been determined to 1.5 A using a combination of molecular-replacement and isomorphous-replacement techniques. Molecular replacement involved a multiparameter search using X-PLOR with two 37-mers of alanine in idealized alpha-helical conformations as the search models. Identified were a large number of potential solutions from which the correct solution was not distinguishable. Commitment of the top 1620 solutions to cycles of rigid-body, positional and simulated-annealing refinement identified the correct solution by a small margin in R factor. Low-resolution electron-density maps generated with phasing information from TbNO(3) and LaNO(3) derivatives were consistent with the top molecular-replacement solution. These derivatives also provided a means to filter and compare the large number of other molecular-replacement solutions with reasonable R factor statistics. The structure-solution strategy described herein may prove useful for the determination of other relatively simple alpha-helical X-ray structures.
DOI: 10.1107/S0907444995015253
PubMed: 15299670
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure determination of a lone alpha-helical antifreeze protein from winter flounder.</title><author><name sortKey="Sicheri, F" sort="Sicheri, F" uniqKey="Sicheri F" first="F" last="Sicheri">F. Sicheri</name><affiliation><nlm:affiliation>Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, D S" sort="Yang, D S" uniqKey="Yang D" first="D S" last="Yang">D S Yang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1996">1996</date><idno type="RBID">pubmed:15299670</idno><idno type="pmid">15299670</idno><idno type="doi">10.1107/S0907444995015253</idno><idno type="wicri:Area/PubMed/Corpus">002775</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002775</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structure determination of a lone alpha-helical antifreeze protein from winter flounder.</title><author><name sortKey="Sicheri, F" sort="Sicheri, F" uniqKey="Sicheri F" first="F" last="Sicheri">F. Sicheri</name><affiliation><nlm:affiliation>Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, D S" sort="Yang, D S" uniqKey="Yang D" first="D S" last="Yang">D S Yang</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The X-ray crystal structure of a lone alpha-helical antifreeze protein from winter flounder has been determined to 1.5 A using a combination of molecular-replacement and isomorphous-replacement techniques. Molecular replacement involved a multiparameter search using X-PLOR with two 37-mers of alanine in idealized alpha-helical conformations as the search models. Identified were a large number of potential solutions from which the correct solution was not distinguishable. Commitment of the top 1620 solutions to cycles of rigid-body, positional and simulated-annealing refinement identified the correct solution by a small margin in R factor. Low-resolution electron-density maps generated with phasing information from TbNO(3) and LaNO(3) derivatives were consistent with the top molecular-replacement solution. These derivatives also provided a means to filter and compare the large number of other molecular-replacement solutions with reasonable R factor statistics. The structure-solution strategy described herein may prove useful for the determination of other relatively simple alpha-helical X-ray structures.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">15299670</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>16</Day></DateCompleted><DateRevised><Year>2007</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>52</Volume><Issue>Pt 3</Issue><PubDate><Year>1996</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr. D Biol. Crystallogr.</ISOAbbreviation></Journal><ArticleTitle>Structure determination of a lone alpha-helical antifreeze protein from winter flounder.</ArticleTitle><Pagination><MedlinePgn>486-98</MedlinePgn></Pagination><Abstract><AbstractText>The X-ray crystal structure of a lone alpha-helical antifreeze protein from winter flounder has been determined to 1.5 A using a combination of molecular-replacement and isomorphous-replacement techniques. Molecular replacement involved a multiparameter search using X-PLOR with two 37-mers of alanine in idealized alpha-helical conformations as the search models. Identified were a large number of potential solutions from which the correct solution was not distinguishable. Commitment of the top 1620 solutions to cycles of rigid-body, positional and simulated-annealing refinement identified the correct solution by a small margin in R factor. Low-resolution electron-density maps generated with phasing information from TbNO(3) and LaNO(3) derivatives were consistent with the top molecular-replacement solution. These derivatives also provided a means to filter and compare the large number of other molecular-replacement solutions with reasonable R factor statistics. The structure-solution strategy described herein may prove useful for the determination of other relatively simple alpha-helical X-ray structures.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sicheri</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>D S</ForeName><Initials>DS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15299670</ArticleId><ArticleId IdType="doi">10.1107/S0907444995015253</ArticleId><ArticleId IdType="pii">S0907444995015253</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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