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Article: Expression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR protein

TitleExpression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR protein
Authors
Kotaka, MDutta, SLee, HCLim, MJWong, YRao, FMitchell, EPLiang, ZXLescar, J
KeywordsEAL-domain proteins
Pseudomonas aeruginosa
RocR
Issue Date2009
PublisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091
Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2009, v. 65 n. 10, p. 1035-1038 How to Cite?
DOI: http://dx.doi.org/10.1107/S1744309109034526
AbstractPseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 A. The crystals belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 118.8, b = 118.8, c = 495.1 A, alpha = beta = 90, gamma = 120 degrees .
Persistent Identifierhttp://hdl.handle.net/10722/124517
ISSN
1744-3091
2014 Impact Factor: 0.524
PubMed Central ID
PMC2765895
ISI Accession Number ID
WOS:000270387700019
Funding AgencyGrant Number
BMRC05/1/22/19/405
06/1/22/19/464
CNRS
Funding Information:

This work was supported by BMRC grants 05/1/22/19/405 (JL) and 06/1/22/19/464 (Z-XL) and an ATIP from CNRS to the laboratory of JL. We are grateful to the staff of NSRRC, Taiwan for generous allocation of beamtime and competent help.

References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorKotaka, Men_HK
dc.contributor.authorDutta, Sen_HK
dc.contributor.authorLee, HCen_HK
dc.contributor.authorLim, MJen_HK
dc.contributor.authorWong, Yen_HK
dc.contributor.authorRao, Fen_HK
dc.contributor.authorMitchell, EPen_HK
dc.contributor.authorLiang, ZXen_HK
dc.contributor.authorLescar, Jen_HK
dc.date.accessioned2010-10-31T10:38:53Z-
dc.date.available2010-10-31T10:38:53Z-
dc.date.issued2009en_HK
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2009, v. 65 n. 10, p. 1035-1038en_HK
dc.identifier.issn1744-3091en_HK
dc.identifier.urihttp://hdl.handle.net/10722/124517-
dc.description.abstractPseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 A. The crystals belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 118.8, b = 118.8, c = 495.1 A, alpha = beta = 90, gamma = 120 degrees .en_HK
dc.languageengen_HK
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091en_HK
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications Onlineen_HK
dc.subjectEAL-domain proteins-
dc.subjectPseudomonas aeruginosa-
dc.subjectRocR-
dc.subject.meshCrystallization-
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshPseudomonas aeruginosa - chemistry-
dc.subject.meshTranscription Factors - chemistry-
dc.titleExpression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR proteinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1744-3091&volume=65&spage=1035&epage=8&date=2009&atitle=Expression,+purification+and+preliminary+crystallographic+analysis+of+Pseudomonas+aeruginosa+RocR+protein.en_HK
dc.identifier.emailKotaka, M: masayo@hku.hken_HK
dc.identifier.emailLescar, J: julien@ntu.edu.sg-
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1107/S1744309109034526en_HK
dc.identifier.pmid19851016-
dc.identifier.pmcidPMC2765895-
dc.identifier.scopuseid_2-s2.0-70350331582en_HK
dc.identifier.hkuros175947en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70350331582&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume65en_HK
dc.identifier.issue10en_HK
dc.identifier.spage1035en_HK
dc.identifier.epage1038en_HK
dc.identifier.isiWOS:000270387700019-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLescar, J=6603844493en_HK
dc.identifier.scopusauthoridLiang, ZX=23668102800en_HK
dc.identifier.scopusauthoridMitchell, EP=7201803888en_HK
dc.identifier.scopusauthoridRao, F=24465697600en_HK
dc.identifier.scopusauthoridWong, Y=35486317500en_HK
dc.identifier.scopusauthoridLim, MJM=35484940100en_HK
dc.identifier.scopusauthoridLee, HC=13806914800en_HK
dc.identifier.scopusauthoridDutta, S=24464182000en_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.citeulike5867014-
dc.identifier.issnl1744-3091-

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