MelampsoraV1, Main, Exploration, bibRecord, 000135

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.

Identifieur interne : 000135 ( Main/Exploration ); précédent : 000134; suivant : 000136

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.

Auteurs : Gregor Guncar [Australie] ; Ching-I A. Wang ; Jade K. Forwood ; Trazel Teh ; Ann-Maree Catanzariti ; Jeffrey G. Ellis ; Peter N. Dodds ; Bostjan Kobe

Source :

Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2007.

RBID : pubmed:17329816

Descripteurs français

KwdFr :
- Basidiomycota (composition chimique), Basidiomycota (pathogénicité), Cobalt (composition chimique), Cristallisation (MeSH), Cristallographie aux rayons X (méthodes), Lin (composition chimique), Lin (microbiologie), Maladies des plantes (microbiologie), Protéines fongiques (composition chimique), Virulence (physiologie).
MESH :
- composition chimique : Basidiomycota, Cobalt, Lin, Protéines fongiques.
- microbiologie : Lin, Maladies des plantes.
- méthodes : Cristallographie aux rayons X.
- pathogénicité : Basidiomycota.
- physiologie : Virulence.
- Cristallisation.

English descriptors

KwdEn :
- Basidiomycota (chemistry), Basidiomycota (pathogenicity), Cobalt (chemistry), Crystallization (MeSH), Crystallography, X-Ray (methods), Flax (chemistry), Flax (microbiology), Fungal Proteins (chemistry), Plant Diseases (microbiology), Virulence (physiology).
MESH :
- chemical , chemistry : Cobalt, Fungal Proteins.
- chemistry : Basidiomycota, Flax.
- methods : Crystallography, X-Ray.
- microbiology : Flax, Plant Diseases.
- pathogenicity : Basidiomycota.
- physiology : Virulence.
- Crystallization.

Abstract

Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based on the anomalous signal of a cobalt ion measured on a conventional monochromatic X-ray source. The unique absorption edge of cobalt (1.61 A) is compatible with the Cu K alpha wavelength (1.54 A) commonly available in macromolecular crystallography laboratories. This approach was applied to the determination of the structure of Melampsora lini avirulence protein AvrL567-A, a protein with a novel fold from the fungal pathogen flax rust that induces plant disease resistance in flax plants. This approach using cobalt ions may be applicable to all cobalt-binding proteins and may be advantageous when synchrotron radiation is not readily available.

DOI: 10.1107/S1744309107004599
PubMed: 17329816
PubMed Central: PMC2330185

Affiliations:

Australie

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000153
to stream Main, to step Curation: 000153

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.</title>
<author><name sortKey="Guncar, Gregor" sort="Guncar, Gregor" uniqKey="Guncar G" first="Gregor" last="Guncar">Gregor Guncar</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072</wicri:regionArea>
<wicri:noRegion>Qld 4072</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Ching I A" sort="Wang, Ching I A" uniqKey="Wang C" first="Ching-I A" last="Wang">Ching-I A. Wang</name>
</author>
<author><name sortKey="Forwood, Jade K" sort="Forwood, Jade K" uniqKey="Forwood J" first="Jade K" last="Forwood">Jade K. Forwood</name>
</author>
<author><name sortKey="Teh, Trazel" sort="Teh, Trazel" uniqKey="Teh T" first="Trazel" last="Teh">Trazel Teh</name>
</author>
<author><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name>
</author>
<author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name>
</author>
<author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name>
</author>
<author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2007">2007</date>
<idno type="RBID">pubmed:17329816</idno>
<idno type="pmid">17329816</idno>
<idno type="doi">10.1107/S1744309107004599</idno>
<idno type="pmc">PMC2330185</idno>
<idno type="wicri:Area/Main/Corpus">000153</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000153</idno>
<idno type="wicri:Area/Main/Curation">000153</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000153</idno>
<idno type="wicri:Area/Main/Exploration">000153</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.</title>
<author><name sortKey="Guncar, Gregor" sort="Guncar, Gregor" uniqKey="Guncar G" first="Gregor" last="Guncar">Gregor Guncar</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072</wicri:regionArea>
<wicri:noRegion>Qld 4072</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Ching I A" sort="Wang, Ching I A" uniqKey="Wang C" first="Ching-I A" last="Wang">Ching-I A. Wang</name>
</author>
<author><name sortKey="Forwood, Jade K" sort="Forwood, Jade K" uniqKey="Forwood J" first="Jade K" last="Forwood">Jade K. Forwood</name>
</author>
<author><name sortKey="Teh, Trazel" sort="Teh, Trazel" uniqKey="Teh T" first="Trazel" last="Teh">Trazel Teh</name>
</author>
<author><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name>
</author>
<author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name>
</author>
<author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name>
</author>
<author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name>
</author>
</analytic>
<series><title level="j">Acta crystallographica. Section F, Structural biology and crystallization communications</title>
<idno type="eISSN">1744-3091</idno>
<imprint><date when="2007" type="published">2007</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (chemistry)</term>
<term>Basidiomycota (pathogenicity)</term>
<term>Cobalt (chemistry)</term>
<term>Crystallization (MeSH)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Flax (chemistry)</term>
<term>Flax (microbiology)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Plant Diseases (microbiology)</term>
<term>Virulence (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (composition chimique)</term>
<term>Basidiomycota (pathogénicité)</term>
<term>Cobalt (composition chimique)</term>
<term>Cristallisation (MeSH)</term>
<term>Cristallographie aux rayons X (méthodes)</term>
<term>Lin (composition chimique)</term>
<term>Lin (microbiologie)</term>
<term>Maladies des plantes (microbiologie)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Virulence (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cobalt</term>
<term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Basidiomycota</term>
<term>Flax</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Basidiomycota</term>
<term>Cobalt</term>
<term>Lin</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Lin</term>
<term>Maladies des plantes</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flax</term>
<term>Plant Diseases</term>
</keywords>
<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virulence</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Virulence</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Crystallization</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cristallisation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based on the anomalous signal of a cobalt ion measured on a conventional monochromatic X-ray source. The unique absorption edge of cobalt (1.61 A) is compatible with the Cu K alpha wavelength (1.54 A) commonly available in macromolecular crystallography laboratories. This approach was applied to the determination of the structure of Melampsora lini avirulence protein AvrL567-A, a protein with a novel fold from the fungal pathogen flax rust that induces plant disease resistance in flax plants. This approach using cobalt ions may be applicable to all cobalt-binding proteins and may be advantageous when synchrotron radiation is not readily available.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17329816</PMID>
<DateCompleted><Year>2007</Year>
<Month>03</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>11</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-3091</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>63</Volume>
<Issue>Pt 3</Issue>
<PubDate><Year>2007</Year>
<Month>Mar</Month>
<Day>01</Day>
</PubDate>
</JournalIssue>
<Title>Acta crystallographica. Section F, Structural biology and crystallization communications</Title>
<ISOAbbreviation>Acta Crystallogr Sect F Struct Biol Cryst Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.</ArticleTitle>
<Pagination><MedlinePgn>209-13</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based on the anomalous signal of a cobalt ion measured on a conventional monochromatic X-ray source. The unique absorption edge of cobalt (1.61 A) is compatible with the Cu K alpha wavelength (1.54 A) commonly available in macromolecular crystallography laboratories. This approach was applied to the determination of the structure of Melampsora lini avirulence protein AvrL567-A, a protein with a novel fold from the fungal pathogen flax rust that induces plant disease resistance in flax plants. This approach using cobalt ions may be applicable to all cobalt-binding proteins and may be advantageous when synchrotron radiation is not readily available.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guncar</LastName>
<ForeName>Gregor</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Ching-I A</ForeName>
<Initials>CI</Initials>
</Author>
<Author ValidYN="Y"><LastName>Forwood</LastName>
<ForeName>Jade K</ForeName>
<Initials>JK</Initials>
</Author>
<Author ValidYN="Y"><LastName>Teh</LastName>
<ForeName>Trazel</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Catanzariti</LastName>
<ForeName>Ann-Maree</ForeName>
<Initials>AM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ellis</LastName>
<ForeName>Jeffrey G</ForeName>
<Initials>JG</Initials>
</Author>
<Author ValidYN="Y"><LastName>Dodds</LastName>
<ForeName>Peter N</ForeName>
<Initials>PN</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kobe</LastName>
<ForeName>Bostjan</ForeName>
<Initials>B</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>2OPC</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2007</Year>
<Month>02</Month>
<Day>23</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Acta Crystallogr Sect F Struct Biol Cryst Commun</MedlineTA>
<NlmUniqueID>101226117</NlmUniqueID>
<ISSNLinking>1744-3091</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>3G0H8C9362</RegistryNumber>
<NameOfSubstance UI="D003035">Cobalt</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003035" MajorTopicYN="N">Cobalt</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019597" MajorTopicYN="N">Flax</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year>
<Month>11</Month>
<Day>14</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2007</Year>
<Month>01</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2007</Year>
<Month>3</Month>
<Day>3</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2007</Year>
<Month>3</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2007</Year>
<Month>3</Month>
<Day>3</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">17329816</ArticleId>
<ArticleId IdType="pii">S1744309107004599</ArticleId>
<ArticleId IdType="doi">10.1107/S1744309107004599</ArticleId>
<ArticleId IdType="pmc">PMC2330185</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):849-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089316</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):191-205</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089410</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 2000 Jan;7(1):53-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10625428</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):965-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10944333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2001 Aug;3(4):625-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11554449</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):494-506</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11856836</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1772-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12351820</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1937-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12393925</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12393927</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Struct Biol. 2002 Oct;12(5):674-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12464322</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16642-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12475936</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1028-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12777766</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Biotechnol. 1992 Aug;3(4):378-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1368439</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1958-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14573950</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1966-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14573951</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2003;374:229-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14696376</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2004 Mar;16(3):755-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14973158</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 2004 May;13(5):1331-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15096636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):849-59</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15103130</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2004 Jul 6;43(26):8346-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15222747</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299926</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2004 Nov 18;432(7015):411-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15549109</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Sep 2;280(35):31249-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15987687</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8888-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16731621</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biochem Parasitol. 2007 Jan;151(1):100-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17125854</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Protein Chem. 1991;42:1-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1793004</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1991 Oct 4;254(5028):51-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1925561</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1975 Jan 14;14(1):97-101</Citation>
<ArticleIdList><ArticleId IdType="pubmed">234019</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1981 Mar 12;290(5802):107-113</Citation>
<ArticleIdList><ArticleId IdType="pubmed">28769131</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1988 Aug 12;241(4867):806-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3406739</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1985;115:90-112</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4079800</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 1972 May 18;263(3):827-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4338312</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1973;40:1-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4588739</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1968 Apr 28;33(2):491-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5700707</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1993;226:52-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8277880</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1997 Sep 1;25(17):3389-402</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9254694</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Australie</li>
</country>
</list>
<tree><noCountry><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name>
<name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name>
<name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name>
<name sortKey="Forwood, Jade K" sort="Forwood, Jade K" uniqKey="Forwood J" first="Jade K" last="Forwood">Jade K. Forwood</name>
<name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name>
<name sortKey="Teh, Trazel" sort="Teh, Trazel" uniqKey="Teh T" first="Trazel" last="Teh">Trazel Teh</name>
<name sortKey="Wang, Ching I A" sort="Wang, Ching I A" uniqKey="Wang C" first="Ching-I A" last="Wang">Ching-I A. Wang</name>
</noCountry>
<country name="Australie"><noRegion><name sortKey="Guncar, Gregor" sort="Guncar, Gregor" uniqKey="Guncar G" first="Gregor" last="Guncar">Gregor Guncar</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/MelampsoraV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000135 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000135 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    MelampsoraV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:17329816
   |texte=   The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:17329816" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a MelampsoraV1

This area was generated with Dilib version V0.6.37.
Data generation: Mon Nov 2 18:19:24 2020. Site generation: Thu Feb 15 23:05:49 2024

	Serveur d'exploration Melampsora
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration Melampsora

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki