Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione.
Identifieur interne : 004470 ( Main/Exploration ); précédent : 004469; suivant : 004471Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione.
Auteurs : Katia D'Ambrosio [France] ; Brice Kauffmann ; Nicolas Rouhier ; Ettore Benedetti ; Jean-Pierre Jacquot ; André Aubry ; Catherine CorbierSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2003.
Descripteurs français
- KwdFr :
- Arbres (MeSH), Clonage moléculaire (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Glutarédoxines (MeSH), Glutathion (composition chimique), Mutagenèse dirigée (MeSH), Oxidoreductases (MeSH), Protéines (composition chimique), Sélénométhionine (composition chimique), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glutathione, Proteins, Selenomethionine.
- chemical : Glutaredoxins, Oxidoreductases.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Mutagenesis, Site-Directed, Trees.
Abstract
A monocysteinic mutant of poplar glutaredoxin (C30S) has been overproduced and purified. The protein has been crystallized in complex with glutathione using the hanging-drop vapour-diffusion technique in the presence of PEG 4000 as a precipitating agent. A native data set was collected at 1.55 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.7, b = 49.1, c = 104.8 A. Isomorphous crystals of a selenomethionine derivative were grown under the same conditions. Three data sets were collected at 1.73 A using the FIP synchrotron beamline at the ESRF. The positions of the Se atoms were determined and model rebuilding and refinement are in progress.
DOI: 10.1107/s0907444903006814
PubMed: 12777768
Affiliations:
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Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="2003" type="published">2003</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>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (chemistry)</term><term>Selenomethionine (chemistry)</term><term>Trees (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arbres (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (composition chimique)</term><term>Sélénométhionine (composition chimique)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione</term><term>Proteins</term><term>Selenomethionine</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathion</term><term>Protéines</term><term>Sélénométhionine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Mutagenesis, Site-Directed</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Arbres</term><term>Clonage moléculaire</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Glutarédoxines</term><term>Mutagenèse dirigée</term><term>Oxidoreductases</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A monocysteinic mutant of poplar glutaredoxin (C30S) has been overproduced and purified. The protein has been crystallized in complex with glutathione using the hanging-drop vapour-diffusion technique in the presence of PEG 4000 as a precipitating agent. A native data set was collected at 1.55 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.7, b = 49.1, c = 104.8 A. Isomorphous crystals of a selenomethionine derivative were grown under the same conditions. Three data sets were collected at 1.73 A using the FIP synchrotron beamline at the ESRF. The positions of the Se atoms were determined and model rebuilding and refinement are in progress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12777768</PMID><DateCompleted><Year>2004</Year><Month>01</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>Pt 6</Issue><PubDate><Year>2003</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione.</ArticleTitle><Pagination><MedlinePgn>1043-5</MedlinePgn></Pagination><Abstract><AbstractText>A monocysteinic mutant of poplar glutaredoxin (C30S) has been overproduced and purified. The protein has been crystallized in complex with glutathione using the hanging-drop vapour-diffusion technique in the presence of PEG 4000 as a precipitating agent. A native data set was collected at 1.55 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.7, b = 49.1, c = 104.8 A. Isomorphous crystals of a selenomethionine derivative were grown under the same conditions. Three data sets were collected at 1.73 A using the FIP synchrotron beamline at the ESRF. The positions of the Se atoms were determined and model rebuilding and refinement are in progress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>D'Ambrosio</LastName><ForeName>Katia</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>LCM3B, Groupe Biocristallographie, UMR CNRS 7036, UHP-Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lès-Nancy CEDEX, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kauffmann</LastName><ForeName>Brice</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Benedetti</LastName><ForeName>Ettore</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Aubry</LastName><ForeName>André</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>05</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>964MRK2PEL</RegistryNumber><NameOfSubstance UI="D012645">Selenomethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</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="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName 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PubStatus="pubmed"><Year>2003</Year><Month>6</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>1</Month><Day>30</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>6</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12777768</ArticleId><ArticleId IdType="pii">S0907444903006814</ArticleId><ArticleId IdType="doi">10.1107/s0907444903006814</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandœuvre-lès-Nancy</li></settlement></list><tree><noCountry><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name><name sortKey="Benedetti, Ettore" sort="Benedetti, Ettore" uniqKey="Benedetti E" first="Ettore" last="Benedetti">Ettore Benedetti</name><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Kauffmann, Brice" sort="Kauffmann, Brice" uniqKey="Kauffmann B" first="Brice" last="Kauffmann">Brice Kauffmann</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="D Ambrosio, Katia" sort="D Ambrosio, Katia" uniqKey="D Ambrosio K" first="Katia" last="D'Ambrosio">Katia D'Ambrosio</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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