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Article: Expression, purification and preliminary X-ray analysis of the BRCT domain from Rhp9/Crb2

TitleExpression, purification and preliminary X-ray analysis of the BRCT domain from Rhp9/Crb2
Authors
Issue Date2003
PublisherInternational Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1
Citation
Acta Crystallographica Section D: Biological Crystallography, 2003, v. 59 n. 7, p. 1230-1233 How to Cite?
AbstractThe BRCT domain from Rhp9 (a Schizosaccharomyces pombe DNA-damage checkpoint protein) has been expressed, purified and crystallized. Overexpression in bacterial cells was achieved by minimizing aeration during host cell growth. A robotic screen was used to determine the solubility parameters; concentration of the protein was achieved by exploiting this information. Single crystals suitable for X-ray analysis were obtained in two forms by vapour diffusion (trigonal, unit-cell parameters a = b = 228.04, c = 70.42 A, and tetragonal, P4/m Laue group symmetry, unit-cell parameters a = b = 72.3, c = 91.1 A).
Persistent Identifierhttp://hdl.handle.net/10722/163627
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHinks, JA-
dc.contributor.authorRoe, M-
dc.contributor.authorHo, JCY-
dc.contributor.authorWatts, FZ-
dc.contributor.authorPhelan, J-
dc.contributor.authorMcAllister, M-
dc.contributor.authorPearl, LH-
dc.date.accessioned2012-09-14T03:32:31Z-
dc.date.available2012-09-14T03:32:31Z-
dc.date.issued2003-
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 2003, v. 59 n. 7, p. 1230-1233-
dc.identifier.issn0907-4449-
dc.identifier.urihttp://hdl.handle.net/10722/163627-
dc.description.abstractThe BRCT domain from Rhp9 (a Schizosaccharomyces pombe DNA-damage checkpoint protein) has been expressed, purified and crystallized. Overexpression in bacterial cells was achieved by minimizing aeration during host cell growth. A robotic screen was used to determine the solubility parameters; concentration of the protein was achieved by exploiting this information. Single crystals suitable for X-ray analysis were obtained in two forms by vapour diffusion (trigonal, unit-cell parameters a = b = 228.04, c = 70.42 A, and tetragonal, P4/m Laue group symmetry, unit-cell parameters a = b = 72.3, c = 91.1 A).-
dc.languageeng-
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1-
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCell Cycle Proteins - chemistry-
dc.subject.meshCloning, Molecular - methods-
dc.subject.meshCrystallization - methods-
dc.subject.meshNuclear Proteins - chemistry-
dc.subject.meshSchizosaccharomyces pombe Proteins - chemistry-
dc.titleExpression, purification and preliminary X-ray analysis of the BRCT domain from Rhp9/Crb2en_US
dc.typeArticleen_US
dc.identifier.emailHo, JCY: jennyho@hku.hk-
dc.identifier.emailPearl, LH: l.pearl@icr.ac.uk-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1107/S0907444903007054-
dc.identifier.pmid12832769-
dc.identifier.scopuseid_2-s2.0-0038455892-
dc.identifier.hkuros82771-
dc.identifier.volume59-
dc.identifier.issue7-
dc.identifier.spage1230-
dc.identifier.epage1233-
dc.identifier.isiWOS:000183809900017-
dc.publisher.placeUnited States-

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