PhanerochaeteV1, Main, Exploration, bibRecord, 000643

Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000643 ( Main/Exploration ); précédent : 000642; suivant : 000644

Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.

Auteurs : Takuya Ishida [Japon] ; Zui Fujimoto ; Hitomi Ichinose ; Kiyohiko Igarashi ; Satoshi Kaneko ; Masahiro Samejima

Source :

Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2009.

RBID : pubmed:20054127

Descripteurs français

KwdFr :
- Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Glycosidases (composition chimique), Glycosidases (génétique), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Pichia (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique).
MESH :
- composition chimique : Glycosidases, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Glycosidases, Phanerochaete, Pichia, Protéines recombinantes.
- métabolisme : Pichia.
- Clonage moléculaire, Conformation des protéines, Cristallisation, Cristallographie aux rayons X.

English descriptors

KwdEn :
- Cloning, Molecular (MeSH), Crystallization (MeSH), Crystallography, X-Ray (MeSH), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Pichia (metabolism), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics).
MESH :
- chemical , chemistry : Glycoside Hydrolases, Recombinant Proteins.
- chemical , genetics : Glycoside Hydrolases, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- metabolism : Pichia.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Protein Conformation.

Abstract

Exo-beta-1,3-galactanase from Phanerochaete chrysosporium (Pc1,3Gal43A) consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35. It catalyzes the hydrolysis of beta-1,3-galactan, which is the backbone of the arabinogalactan proteins; the C-terminal carbohydrate-binding module family 35 domain increases the local concentration of the enzyme around beta-1,3-galactan by its high affinity for the substrate. To enable phase determination using the multiwavelength anomalous dispersion method, selenomethionyl Pc1,3Gal43A was crystallized at 298 K using the hanging-drop vapour-diffusion method. The presence of selenium in the crystals was confirmed from the X-ray absorption spectrum. The crystals belonged to space group P2(1) and diffracted to 1.8 A resolution.

DOI: 10.1107/S1744309109043395
PubMed: 20054127
PubMed Central: PMC2802879

Affiliations:

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

to stream Main, to step Corpus: 000584
to stream Main, to step Curation: 000584

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.</title>
<author><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
<orgName type="university">Université de Tokyo</orgName>
</affiliation>
</author>
<author><name sortKey="Fujimoto, Zui" sort="Fujimoto, Zui" uniqKey="Fujimoto Z" first="Zui" last="Fujimoto">Zui Fujimoto</name>
</author>
<author><name sortKey="Ichinose, Hitomi" sort="Ichinose, Hitomi" uniqKey="Ichinose H" first="Hitomi" last="Ichinose">Hitomi Ichinose</name>
</author>
<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
</author>
<author><name sortKey="Kaneko, Satoshi" sort="Kaneko, Satoshi" uniqKey="Kaneko S" first="Satoshi" last="Kaneko">Satoshi Kaneko</name>
</author>
<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2009">2009</date>
<idno type="RBID">pubmed:20054127</idno>
<idno type="pmid">20054127</idno>
<idno type="doi">10.1107/S1744309109043395</idno>
<idno type="pmc">PMC2802879</idno>
<idno type="wicri:Area/Main/Corpus">000584</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000584</idno>
<idno type="wicri:Area/Main/Curation">000584</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000584</idno>
<idno type="wicri:Area/Main/Exploration">000584</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.</title>
<author><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
<orgName type="university">Université de Tokyo</orgName>
</affiliation>
</author>
<author><name sortKey="Fujimoto, Zui" sort="Fujimoto, Zui" uniqKey="Fujimoto Z" first="Zui" last="Fujimoto">Zui Fujimoto</name>
</author>
<author><name sortKey="Ichinose, Hitomi" sort="Ichinose, Hitomi" uniqKey="Ichinose H" first="Hitomi" last="Ichinose">Hitomi Ichinose</name>
</author>
<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
</author>
<author><name sortKey="Kaneko, Satoshi" sort="Kaneko, Satoshi" uniqKey="Kaneko S" first="Satoshi" last="Kaneko">Satoshi Kaneko</name>
</author>
<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</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="2009" type="published">2009</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term>
<term>Crystallization (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Glycoside Hydrolases (chemistry)</term>
<term>Glycoside Hydrolases (genetics)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Pichia (genetics)</term>
<term>Pichia (metabolism)</term>
<term>Protein Conformation (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cristallisation (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Glycosidases (composition chimique)</term>
<term>Glycosidases (génétique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Pichia (génétique)</term>
<term>Pichia (métabolisme)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycoside Hydrolases</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycoside Hydrolases</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycosidases</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term>
<term>Pichia</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycosidases</term>
<term>Phanerochaete</term>
<term>Pichia</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pichia</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Pichia</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term>
<term>Crystallization</term>
<term>Crystallography, X-Ray</term>
<term>Protein Conformation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term>
<term>Conformation des protéines</term>
<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Exo-beta-1,3-galactanase from Phanerochaete chrysosporium (Pc1,3Gal43A) consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35. It catalyzes the hydrolysis of beta-1,3-galactan, which is the backbone of the arabinogalactan proteins; the C-terminal carbohydrate-binding module family 35 domain increases the local concentration of the enzyme around beta-1,3-galactan by its high affinity for the substrate. To enable phase determination using the multiwavelength anomalous dispersion method, selenomethionyl Pc1,3Gal43A was crystallized at 298 K using the hanging-drop vapour-diffusion method. The presence of selenium in the crystals was confirmed from the X-ray absorption spectrum. The crystals belonged to space group P2(1) and diffracted to 1.8 A resolution.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20054127</PMID>
<DateCompleted><Year>2010</Year>
<Month>03</Month>
<Day>19</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>08</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-3091</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>65</Volume>
<Issue>Pt 12</Issue>
<PubDate><Year>2009</Year>
<Month>Dec</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>Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle>
<Pagination><MedlinePgn>1274-6</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1107/S1744309109043395</ELocationID>
<Abstract><AbstractText>Exo-beta-1,3-galactanase from Phanerochaete chrysosporium (Pc1,3Gal43A) consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35. It catalyzes the hydrolysis of beta-1,3-galactan, which is the backbone of the arabinogalactan proteins; the C-terminal carbohydrate-binding module family 35 domain increases the local concentration of the enzyme around beta-1,3-galactan by its high affinity for the substrate. To enable phase determination using the multiwavelength anomalous dispersion method, selenomethionyl Pc1,3Gal43A was crystallized at 298 K using the hanging-drop vapour-diffusion method. The presence of selenium in the crystals was confirmed from the X-ray absorption spectrum. The crystals belonged to space group P2(1) and diffracted to 1.8 A resolution.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ishida</LastName>
<ForeName>Takuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fujimoto</LastName>
<ForeName>Zui</ForeName>
<Initials>Z</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ichinose</LastName>
<ForeName>Hitomi</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Igarashi</LastName>
<ForeName>Kiyohiko</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kaneko</LastName>
<ForeName>Satoshi</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Samejima</LastName>
<ForeName>Masahiro</ForeName>
<Initials>M</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2009</Year>
<Month>11</Month>
<Day>27</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="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber>
<NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber>
<NameOfSubstance UI="C547834">selenomethionyl exo-beta-1,3-galactanase, Phanerochaete chrysosporium</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year>
<Month>09</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2009</Year>
<Month>10</Month>
<Day>21</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2010</Year>
<Month>1</Month>
<Day>8</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>1</Month>
<Day>8</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>3</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">20054127</ArticleId>
<ArticleId IdType="pii">S1744309109043395</ArticleId>
<ArticleId IdType="doi">10.1107/S1744309109043395</ArticleId>
<ArticleId IdType="pmc">PMC2802879</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Plant Mol Biol. 2001 Sep;47(1-2):161-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11554470</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):346-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11807273</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 2002 Sep;9(9):665-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12198486</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Jul 8;280(27):25820-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15866877</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2006 May 26;359(1):97-109</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16631196</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Plant Biol. 2007;58:137-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17201686</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt 8):692-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17671370</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2009 Jan;37(Database issue):D233-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18838391</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2009 Feb 15;418(1):39-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18980579</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Apr 10;284(15):10100-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19193645</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):632-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19478450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 1974 Jun;139(3):535-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4850989</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1968 Apr 28;33(2):491-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5700707</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Japon</li>
</country>
<region><li>Région de Kantō</li>
</region>
<settlement><li>Tokyo</li>
</settlement>
<orgName><li>Université de Tokyo</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Fujimoto, Zui" sort="Fujimoto, Zui" uniqKey="Fujimoto Z" first="Zui" last="Fujimoto">Zui Fujimoto</name>
<name sortKey="Ichinose, Hitomi" sort="Ichinose, Hitomi" uniqKey="Ichinose H" first="Hitomi" last="Ichinose">Hitomi Ichinose</name>
<name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
<name sortKey="Kaneko, Satoshi" sort="Kaneko, Satoshi" uniqKey="Kaneko S" first="Satoshi" last="Kaneko">Satoshi Kaneko</name>
<name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
</noCountry>
<country name="Japon"><region name="Région de Kantō"><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000643 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000643 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    PhanerochaeteV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:20054127
   |texte=   Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:20054127" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a PhanerochaeteV1

This area was generated with Dilib version V0.6.37.
Data generation: Fri Nov 13 18:33:39 2020. Site generation: Fri Nov 13 18:35:20 2020

	Serveur d'exploration sur le phanerochaete
	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 sur le phanerochaete

Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.

Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.

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