Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar.
Identifieur interne : 004609 ( Main/Exploration ); précédent : 004608; suivant : 004610Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar.
Auteurs : Aude Echalier [France] ; Catherine Corbier ; Nicolas Rouhier ; Jean Pierre Jacquot ; André AubrySource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2002.
Descripteurs français
- KwdFr :
- Arbres (enzymologie), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxirédoxines (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique).
- MESH :
- composition chimique : Peroxidases, Protéines recombinantes.
- enzymologie : Arbres.
- génétique : Peroxidases, Protéines recombinantes.
- Clonage moléculaire, Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Peroxirédoxines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peroxidases, Recombinant Proteins.
- chemical , genetics : Peroxidases, Recombinant Proteins.
- enzymology : Trees.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Peroxiredoxins, Protein Conformation.
Abstract
Two variants (wild type and V152C mutant) of a bifunctional poplar peroxiredoxin have been overexpressed in Escherichia coli cells. The two recombinant enzymes were purified and crystallized using the hanging-drop vapour-diffusion technique. Data sets were collected to 1.62 and 2.48 A resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2(1) (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 A, beta = 93.45 degrees ) and to the orthorhombic space group P2(1)2(1)2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 A), respectively. Data were also collected to 2.17 A resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress.
DOI: 10.1107/S0907444902011782
PubMed: 12198315
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The two recombinant enzymes were purified and crystallized using the hanging-drop vapour-diffusion technique. Data sets were collected to 1.62 and 2.48 A resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2(1) (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 A, beta = 93.45 degrees ) and to the orthorhombic space group P2(1)2(1)2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 A), respectively. Data were also collected to 2.17 A resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12198315</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>58</Volume><Issue>Pt 9</Issue><PubDate><Year>2002</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Acta crystallographica. 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Data were also collected to 2.17 A resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Echalier</LastName><ForeName>Aude</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre CEDEX, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</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></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>08</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="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</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="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></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><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>04</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2002</Year><Month>07</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>8</Month><Day>29</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>2</Month><Day>14</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>8</Month><Day>29</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12198315</ArticleId><ArticleId IdType="doi">10.1107/S0907444902011782</ArticleId><ArticleId IdType="pii">S0907444902011782</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandoeuvre</li></settlement></list><tree><noCountry><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</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="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="Echalier, Aude" sort="Echalier, Aude" uniqKey="Echalier A" first="Aude" last="Echalier">Aude Echalier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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