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Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli
dc.contributor.authorLuschinsky, Catherine L.en_US
dc.contributor.authorDrummond, James T.en_US
dc.contributor.authorMatthews, Rowena Greenen_US
dc.contributor.authorLudwig, Martha L.en_US
dc.date.accessioned2006-04-10T15:13:10Z
dc.date.available2006-04-10T15:13:10Z
dc.date.issued1992-05-20en_US
dc.identifier.citationLuschinsky, Catherine L., Drummond, James T., Matthews, Rowena G., Ludwig, Martha L. (1992/05/20)."Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli." Journal of Molecular Biology 225(2): 557-560. <http://hdl.handle.net/2027.42/30045>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WK7-4DN90RV-TY/2/53a4e517eab2b1f59dcdad17ef7dadf8en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/30045
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1593636&dopt=citationen_US
dc.description.abstractCrystals of a cobalamin-binding domain (Mr = 28,000) have been grown in polyethylene glycol 6000 at pH 7.5, starting from solutions of intact (Mr = 133,000) cobalamin-dependent methionine synthase. The crystals are orthorhombic in space group P212121, with cell dimensions a = 96.9 A, B = 55.4 A, C = 103.8 A. For two molecules per asymmetric unit, the calculated Vm value is 2.45 A3/Da. A native data set has been collected to 3 A resolution.en_US
dc.format.extent1184794 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCrystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia colien_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, MI 48109-2099, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, MI 48109-2099, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, MI 48109-2099, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, MI 48109-2099, U.S.A.en_US
dc.identifier.pmid1593636en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/30045/1/0000413.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0022-2836(92)90940-Len_US
dc.identifier.sourceJournal of Molecular Biologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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