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Article: Structure determination of a 16.8 kDa copper protein at 2.1 a resolution using anomalous scattering data with direct methods

TitleStructure determination of a 16.8 kDa copper protein at 2.1 a resolution using anomalous scattering data with direct methods
Authors
Issue Date1998
PublisherWiley-Blackwell Publishing, Inc.. 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, 1998, v. 54 n. 4, p. 629-635 How to Cite?
AbstractThe structure of rusticyanin, an acid-stable copper protein, has been determined at 2.1 Å resolution by direct methods combined with the single-wavelength anomalous scattering (SAS) of copper (f″ = 3.9 e-) and then conventionally refined (Rcryst = 18.7%, Rfree = 21.9%). This is the largest unknown protein structure (Mr ≃ 16.8 kDa) to be determined using the SAS and direct-methods approach and demonstrates that by exploiting the anomalous signal at a single wavelength, direct methods can be used to determine phases at typical (∼2 Å) macromolecular crystallographic resolutions. Extrapolating from the size of the anomalous signal for copper (f″ ≃ 4 e-), this result suggests that the approach could be used for proteins with molecular weights of up to 33 kDa per Se (f″max = 8 e- at the 'white line') and 80 kDa for a Pt derivative (f″max = 19 e- at the 'white line', L3 edge). The method provides a powerful alternative in solving a de novo protein structure without either preparing multiple crystals (i.e. isomorphous heavy-atom derivative plus native crystals) or collecting multi-wavelength anomalous diffraction (MAD) data. © 1998 International Union of Crystallography all rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91923
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHarvey, Ien_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorDuke, EMHen_HK
dc.contributor.authorIngledew, WJen_HK
dc.contributor.authorHasnain, SSen_HK
dc.date.accessioned2010-09-17T10:30:39Z-
dc.date.available2010-09-17T10:30:39Z-
dc.date.issued1998en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 1998, v. 54 n. 4, p. 629-635en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91923-
dc.description.abstractThe structure of rusticyanin, an acid-stable copper protein, has been determined at 2.1 Å resolution by direct methods combined with the single-wavelength anomalous scattering (SAS) of copper (f″ = 3.9 e-) and then conventionally refined (Rcryst = 18.7%, Rfree = 21.9%). This is the largest unknown protein structure (Mr ≃ 16.8 kDa) to be determined using the SAS and direct-methods approach and demonstrates that by exploiting the anomalous signal at a single wavelength, direct methods can be used to determine phases at typical (∼2 Å) macromolecular crystallographic resolutions. Extrapolating from the size of the anomalous signal for copper (f″ ≃ 4 e-), this result suggests that the approach could be used for proteins with molecular weights of up to 33 kDa per Se (f″max = 8 e- at the 'white line') and 80 kDa for a Pt derivative (f″max = 19 e- at the 'white line', L3 edge). The method provides a powerful alternative in solving a de novo protein structure without either preparing multiple crystals (i.e. isomorphous heavy-atom derivative plus native crystals) or collecting multi-wavelength anomalous diffraction (MAD) data. © 1998 International Union of Crystallography all rights reserved.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1en_HK
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallographyen_HK
dc.titleStructure determination of a 16.8 kDa copper protein at 2.1 a resolution using anomalous scattering data with direct methodsen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S0907444998005423-
dc.identifier.pmid9761859-
dc.identifier.scopuseid_2-s2.0-0032128139en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032128139&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume54en_HK
dc.identifier.issue4en_HK
dc.identifier.spage629en_HK
dc.identifier.epage635en_HK
dc.identifier.isiWOS:000074962500017-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridHarvey, I=35944665600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridDuke, EMH=7005322569en_HK
dc.identifier.scopusauthoridIngledew, WJ=35556236300en_HK
dc.identifier.scopusauthoridHasnain, SS=7102767936en_HK

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