The influence of an internal electric field upon protein crystallization using the gel-acupuncture method.
Identifieur interne : 000466 ( Main/Corpus ); précédent : 000465; suivant : 000467The influence of an internal electric field upon protein crystallization using the gel-acupuncture method.
Auteurs : N. Mirkin ; B A Frontana-Uribe ; A. Rodríguez-Romero ; A. Hernández-Santoyo ; A. MorenoSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2003.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Muramidase, Plant Proteins, Proteins.
- instrumentation : Crystallization.
- methods : Crystallization, Electrochemistry, X-Ray Diffraction.
- Electrodes, Protein Conformation.
Abstract
In this work, the influence of an internal electric field upon the crystallization of lysozyme and thaumatin is explored using a modified design of the gel-acupuncture setup. From a crystallographic point of view, the orientation of crystals that grow preferentially over different types of electrodes inside capillary tubes is also evaluated. Finally, the crystal quality and the three-dimensional structure of these proteins grown with and without the electric field influence are analyzed by means of X-ray diffraction methods.
DOI: 10.1107/s0907444903013027
PubMed: 12925781
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pubmed:12925781Le document en format XML
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Finally, the crystal quality and the three-dimensional structure of these proteins grown with and without the electric field influence are analyzed by means of X-ray diffraction methods.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mirkin</LastName><ForeName>N</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Instituto de Química, UNAM Circuito Exterior, C. U. Mexico, D. F. 04510, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Frontana-Uribe</LastName><ForeName>B A</ForeName><Initials>BA</Initials></Author><Author ValidYN="Y"><LastName>Rodríguez-Romero</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Hernández-Santoyo</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Moreno</LastName><ForeName>A</ForeName><Initials>A</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>2003</Year><Month>08</Month><Day>19</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="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.17</RegistryNumber><NameOfSubstance UI="D009113">Muramidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="N">instrumentation</QualifierName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004563" MajorTopicYN="N">Electrochemistry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004566" MajorTopicYN="N">Electrodes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009113" MajorTopicYN="N">Muramidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>09</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2003</Year><Month>06</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>8</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>6</Month><Day>2</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>8</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12925781</ArticleId><ArticleId IdType="pii">S0907444903013027</ArticleId><ArticleId IdType="doi">10.1107/s0907444903013027</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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