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Article: Combining solution wide-angle X-ray scattering and crystallography: Determination of molecular envelope and heavy-atom sites

TitleCombining solution wide-angle X-ray scattering and crystallography: Determination of molecular envelope and heavy-atom sites
Authors
KeywordsHeavy-atom location
Molecular envelopes
Molecular replacement
Small-angle X-ray scattering (SAXS)
Wide-angle X-ray scattering (WAXS)
Issue Date2009
PublisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JCR
Citation
Journal Of Applied Crystallography, 2009, v. 42 n. 2, p. 259-264 How to Cite?
AbstractSolving the phase problem remains central to crystallographic structure determination. A six-dimensional search method of molecular replacement (FSEARCH) can be used to locate a low-resolution molecular envelope determined from small-angle X-ray scattering (SAXS) within the crystallographic unit cell. This method has now been applied using the higher-resolution envelope provided by combining SAXS and WAXS (wide-angle X-ray scattering) data. The method was tested on horse hemoglobin, using the most probable model selected from a set of a dozen bead models constructed from SAXS/WAXS data using the program GASBOR at 5 Å resolution (q max = 1.25 Å -1) to phase a set of single-crystal diffraction data. It was found that inclusion of WAXS data is essential for correctly locating the molecular envelope in the crystal unit cell, as well as for locating heavy-atom sites. An anomalous difference map was calculated using phases out to 8 Å resolution from the correctly positioned envelope; four distinct peaks at the 3.2σ level were identified, which agree well with the four iron sites of the known structure (Protein Data Bank code 1ns9). In contrast, no peaks could be found close to the iron sites if the molecular envelope was constructed using the data from SAXS alone (q max = 0.25 Å -1). The initial phases can be used as a starting point for a variety of phase-extension techniques, successful application of which will result in complete phasing of a crystallographic data set and determination of the internal structure of a macromolecule to atomic resolution. It is anticipated that the combination of FSEARCH and WAXS techniques will facilitate the initial structure determination of proteins and provide a good foundation for further structure refinement. © International Union of Crystallography 2009.
Persistent Identifierhttp://hdl.handle.net/10722/91907
ISSN
2014 Impact Factor: 3.984
2015 SCImago Journal Rankings: 2.373
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHong, Xen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:11Z-
dc.date.available2010-09-17T10:30:11Z-
dc.date.issued2009en_HK
dc.identifier.citationJournal Of Applied Crystallography, 2009, v. 42 n. 2, p. 259-264en_HK
dc.identifier.issn0021-8898en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91907-
dc.description.abstractSolving the phase problem remains central to crystallographic structure determination. A six-dimensional search method of molecular replacement (FSEARCH) can be used to locate a low-resolution molecular envelope determined from small-angle X-ray scattering (SAXS) within the crystallographic unit cell. This method has now been applied using the higher-resolution envelope provided by combining SAXS and WAXS (wide-angle X-ray scattering) data. The method was tested on horse hemoglobin, using the most probable model selected from a set of a dozen bead models constructed from SAXS/WAXS data using the program GASBOR at 5 Å resolution (q max = 1.25 Å -1) to phase a set of single-crystal diffraction data. It was found that inclusion of WAXS data is essential for correctly locating the molecular envelope in the crystal unit cell, as well as for locating heavy-atom sites. An anomalous difference map was calculated using phases out to 8 Å resolution from the correctly positioned envelope; four distinct peaks at the 3.2σ level were identified, which agree well with the four iron sites of the known structure (Protein Data Bank code 1ns9). In contrast, no peaks could be found close to the iron sites if the molecular envelope was constructed using the data from SAXS alone (q max = 0.25 Å -1). The initial phases can be used as a starting point for a variety of phase-extension techniques, successful application of which will result in complete phasing of a crystallographic data set and determination of the internal structure of a macromolecule to atomic resolution. It is anticipated that the combination of FSEARCH and WAXS techniques will facilitate the initial structure determination of proteins and provide a good foundation for further structure refinement. © International Union of Crystallography 2009.en_HK
dc.languageengen_HK
dc.publisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JCRen_HK
dc.relation.ispartofJournal of Applied Crystallographyen_HK
dc.subjectHeavy-atom locationen_HK
dc.subjectMolecular envelopesen_HK
dc.subjectMolecular replacementen_HK
dc.subjectSmall-angle X-ray scattering (SAXS)en_HK
dc.subjectWide-angle X-ray scattering (WAXS)en_HK
dc.titleCombining solution wide-angle X-ray scattering and crystallography: Determination of molecular envelope and heavy-atom sitesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8898&volume=42&spage=259&epage=264&date=2009&atitle=Combining+solution+wide-angle+X-ray+scattering+and+crystallography:+determination+of+molecular+envelope+and+heavy-atom+sites-
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S0021889809003094en_HK
dc.identifier.pmid19529837-
dc.identifier.pmcidPMC2677545-
dc.identifier.scopuseid_2-s2.0-62649089709en_HK
dc.identifier.hkuros155963-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-62649089709&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume42en_HK
dc.identifier.issue2en_HK
dc.identifier.spage259en_HK
dc.identifier.epage264en_HK
dc.identifier.isiWOS:000264292800015-
dc.publisher.placeDenmarken_HK
dc.identifier.scopusauthoridHong, X=7201551709en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.citeulike4023835-

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