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Article: Use of single isomorphous replacement data of proteins - Resolving the phase ambiguity and a new procedure for phase extension

TitleUse of single isomorphous replacement data of proteins - Resolving the phase ambiguity and a new procedure for phase extension
Authors
Issue Date1997
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, 1997, v. 53 n. 1, p. 49-55 How to Cite?
AbstractA procedure combining direct methods and solvent flattening to break the phase ambiguity intrinsic to the single isomorphous replacement (SIR) technique has been tested with the experimental SIR data of the known protein RNase Sa at 2.5 Å resolution. The use of direct methods provided better initial phases for the solvent-flattening procedure, while the solvent-flattening procedure greatly improved direct-method phases leading to a traceable Fourier map. A small subset of known phases at low resolution makes direct phasing of SIR data much easier. Accordingly a method for extending low-resolution phases to high-resolution ones is proposed making use of additional SIR information. This reduces the problem of finding a value in the range of 0-2π for each unknown phase to that of just making a choice between two possible values. Tests with the known protein RNase Sa showed that the method is able to extend phases from a resolution of 6 to 2.5 Å leading to an easily traceable Fourier map. The solvent-flattening technique and the combination of which with direct methods were used for the phase extension. Either procedure yielded reasonably good results, but on the whole, the result from the combination of direct methods with solvent flattening is better. Results of the latter procedure were further compared with that from direct phasing of the 2.5 Å SIR data and with that from phase extension by solvent flattening without SIR information. An improvement gained by the use of SIR information is evident.
Persistent Identifierhttp://hdl.handle.net/10722/91924
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZheng, XFen_HK
dc.contributor.authorZheng, CDen_HK
dc.contributor.authorGu, YXen_HK
dc.contributor.authorMo, YDen_HK
dc.contributor.authorFan, HFen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:41Z-
dc.date.available2010-09-17T10:30:41Z-
dc.date.issued1997en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 1997, v. 53 n. 1, p. 49-55en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91924-
dc.description.abstractA procedure combining direct methods and solvent flattening to break the phase ambiguity intrinsic to the single isomorphous replacement (SIR) technique has been tested with the experimental SIR data of the known protein RNase Sa at 2.5 Å resolution. The use of direct methods provided better initial phases for the solvent-flattening procedure, while the solvent-flattening procedure greatly improved direct-method phases leading to a traceable Fourier map. A small subset of known phases at low resolution makes direct phasing of SIR data much easier. Accordingly a method for extending low-resolution phases to high-resolution ones is proposed making use of additional SIR information. This reduces the problem of finding a value in the range of 0-2π for each unknown phase to that of just making a choice between two possible values. Tests with the known protein RNase Sa showed that the method is able to extend phases from a resolution of 6 to 2.5 Å leading to an easily traceable Fourier map. The solvent-flattening technique and the combination of which with direct methods were used for the phase extension. Either procedure yielded reasonably good results, but on the whole, the result from the combination of direct methods with solvent flattening is better. Results of the latter procedure were further compared with that from direct phasing of the 2.5 Å SIR data and with that from phase extension by solvent flattening without SIR information. An improvement gained by the use of SIR information is evident.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.titleUse of single isomorphous replacement data of proteins - Resolving the phase ambiguity and a new procedure for phase extensionen_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/S0907444996009365en_HK
dc.identifier.scopuseid_2-s2.0-0030939719en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030939719&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume53en_HK
dc.identifier.issue1en_HK
dc.identifier.spage49en_HK
dc.identifier.epage55en_HK
dc.identifier.isiWOS:A1997WJ22100004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZheng, XF=36766092600en_HK
dc.identifier.scopusauthoridZheng, CD=7401934929en_HK
dc.identifier.scopusauthoridGu, YX=7403046284en_HK
dc.identifier.scopusauthoridMo, YD=7202961906en_HK
dc.identifier.scopusauthoridFan, HF=7402554116en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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