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Article: Accurate and highly complete synchrotron protein crystal Laue diffraction data using the ESRF CCD and the Daresbury Laue software

TitleAccurate and highly complete synchrotron protein crystal Laue diffraction data using the ESRF CCD and the Daresbury Laue software
Authors
KeywordsCCD Laue data
Detector dynamic range
Hydroxymethylbilane synthase
Laue software
Protein crystallography
Issue Date1999
PublisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JSY
Citation
Journal Of Synchrotron Radiation, 1999, v. 6 n. 5, p. 995-1006 How to Cite?
AbstractDevelopments in electronic area detectors such as CCDs and image plates have transformed the capability of the synchrotron Laue protein crystallography technique compared with film. The rapid readout of CCDs makes practical the use of rather fine angular interval settings of the crystal between each Laue exposure and a large overall angle coverage. The use of the ESRF CCD (image intensifier type) presented here in the Laue data collection on ESRF ID09 (the 'Laue beamline') from a single crystal of the 34 kDa wild-type hydroxymethylbilane synthase (HMBS), space group P2 12 12 a = 88.06, b = 75.73, c = 50.35 Å, yielded 47 Laue exposures in 2.5° angle intervals from a single crystal. The data processed by the Daresbury Laue software is highly complete (∞-2d min = 77.5%; 2d min-d min = 91.7%) to 2.3 Å with high redundancy (11.2). Comparison with calculated structure factors and careful analysis of the Laue geometry shows that between ∞ and 5d min better completeness still should be possible, which can ideally be realized from CCD detector dynamic range hardware improvements and/or software algorithms to integrate saturated spot profiles. Prospects for Laue diffraction data collection using yet faster detectors such as the 'pixel detector' to study irreversible catalytic structural processes in a crystal, the most challenging of all time-resolved experiments, are bright.
Persistent Identifierhttp://hdl.handle.net/10722/91895
ISSN
2014 Impact Factor: 2.794
2015 SCImago Journal Rankings: 1.211
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNieh, YPen_HK
dc.contributor.authorRaftery, Jen_HK
dc.contributor.authorWeisgerber, Sen_HK
dc.contributor.authorHabash, Jen_HK
dc.contributor.authorSchotte, Fen_HK
dc.contributor.authorUrsby, Ten_HK
dc.contributor.authorWulff, Men_HK
dc.contributor.authorHädener, Aen_HK
dc.contributor.authorCampbell, JWen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorHelliwell, JRen_HK
dc.date.accessioned2010-09-17T10:29:49Z-
dc.date.available2010-09-17T10:29:49Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Synchrotron Radiation, 1999, v. 6 n. 5, p. 995-1006en_HK
dc.identifier.issn0909-0495en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91895-
dc.description.abstractDevelopments in electronic area detectors such as CCDs and image plates have transformed the capability of the synchrotron Laue protein crystallography technique compared with film. The rapid readout of CCDs makes practical the use of rather fine angular interval settings of the crystal between each Laue exposure and a large overall angle coverage. The use of the ESRF CCD (image intensifier type) presented here in the Laue data collection on ESRF ID09 (the 'Laue beamline') from a single crystal of the 34 kDa wild-type hydroxymethylbilane synthase (HMBS), space group P2 12 12 a = 88.06, b = 75.73, c = 50.35 Å, yielded 47 Laue exposures in 2.5° angle intervals from a single crystal. The data processed by the Daresbury Laue software is highly complete (∞-2d min = 77.5%; 2d min-d min = 91.7%) to 2.3 Å with high redundancy (11.2). Comparison with calculated structure factors and careful analysis of the Laue geometry shows that between ∞ and 5d min better completeness still should be possible, which can ideally be realized from CCD detector dynamic range hardware improvements and/or software algorithms to integrate saturated spot profiles. Prospects for Laue diffraction data collection using yet faster detectors such as the 'pixel detector' to study irreversible catalytic structural processes in a crystal, the most challenging of all time-resolved experiments, are bright.en_HK
dc.languageengen_HK
dc.publisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JSYen_HK
dc.relation.ispartofJournal of Synchrotron Radiationen_HK
dc.subjectCCD Laue dataen_HK
dc.subjectDetector dynamic rangeen_HK
dc.subjectHydroxymethylbilane synthaseen_HK
dc.subjectLaue softwareen_HK
dc.subjectProtein crystallographyen_HK
dc.titleAccurate and highly complete synchrotron protein crystal Laue diffraction data using the ESRF CCD and the Daresbury Laue softwareen_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/s0909049599006342en_US
dc.identifier.scopuseid_2-s2.0-0033436650en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033436650&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume6en_HK
dc.identifier.issue5en_HK
dc.identifier.spage995en_HK
dc.identifier.epage1006en_HK
dc.identifier.isiWOS:000082782600009-
dc.publisher.placeDenmarken_HK
dc.identifier.scopusauthoridNieh, YP=6602331379en_HK
dc.identifier.scopusauthoridRaftery, J=7004558116en_HK
dc.identifier.scopusauthoridWeisgerber, S=7801645652en_HK
dc.identifier.scopusauthoridHabash, J=35587202900en_HK
dc.identifier.scopusauthoridSchotte, F=35507925800en_HK
dc.identifier.scopusauthoridUrsby, T=6604025140en_HK
dc.identifier.scopusauthoridWulff, M=7007128964en_HK
dc.identifier.scopusauthoridHädener, A=6602812829en_HK
dc.identifier.scopusauthoridCampbell, JW=7404877778en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridHelliwell, JR=8693358800en_HK

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