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Article: Estimating unobserved reflection intensities in Laue diffraction by the maximum-entropy method

TitleEstimating unobserved reflection intensities in Laue diffraction by the maximum-entropy method
Authors
Issue Date1999
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, 1999, v. 55 n. 1, p. 238-242 How to Cite?
AbstractIn protein crystallography, the use of low-resolution reflections is important in defining the molecular mask and polypeptide backbone. However, in Laue data collection, the loss of low-resolution reflection data (>2d(min)) can be as high as 40-50%, even after the deconvolution of multiples. To estimate the reflection intensities that are not recorded in data collection, a new method is presented based on maximizing the entropy of the Patterson function subject to the constraints imposed by the intensities of the observed reflections. The method has been tested with Laue diffraction data from hen egg-white lysozyme. All unobserved reflections within 5 Å resolution were estimated, and their inclusion in the electrondensity-map calculation significantly improved the connectivity. This method could also be applied to improve the completeness of monochromatic data.
Persistent Identifierhttp://hdl.handle.net/10722/91914
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXie, Yen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:23Z-
dc.date.available2010-09-17T10:30:23Z-
dc.date.issued1999en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 1999, v. 55 n. 1, p. 238-242en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91914-
dc.description.abstractIn protein crystallography, the use of low-resolution reflections is important in defining the molecular mask and polypeptide backbone. However, in Laue data collection, the loss of low-resolution reflection data (>2d(min)) can be as high as 40-50%, even after the deconvolution of multiples. To estimate the reflection intensities that are not recorded in data collection, a new method is presented based on maximizing the entropy of the Patterson function subject to the constraints imposed by the intensities of the observed reflections. The method has been tested with Laue diffraction data from hen egg-white lysozyme. All unobserved reflections within 5 Å resolution were estimated, and their inclusion in the electrondensity-map calculation significantly improved the connectivity. This method could also be applied to improve the completeness of monochromatic data.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.titleEstimating unobserved reflection intensities in Laue diffraction by the maximum-entropy methoden_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/s0907444998010038en_US
dc.identifier.pmid10089415-
dc.identifier.scopuseid_2-s2.0-0032945310en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032945310&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume55en_HK
dc.identifier.issue1en_HK
dc.identifier.spage238en_HK
dc.identifier.epage242en_HK
dc.identifier.isiWOS:000078314000029-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridXie, Y=7403958892en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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