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dc.contributor.authorMARTIN, JL
dc.contributor.authorWAKSMAN, G
dc.contributor.authorBARDWELL, JCA
dc.contributor.authorBECKWITH, J
dc.contributor.authorKURIYAN, J
dc.date.accessioned2017-10-05T03:42:24Z
dc.date.available2017-10-05T03:42:24Z
dc.date.issued1993
dc.identifier.issn0022-2836
dc.identifier.doi10.1006/jmbi.1993.1226
dc.identifier.urihttp://hdl.handle.net/10072/347918
dc.description.abstractDsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli. Crystals of oxidized DsbA have been obtained from polyethylene glycol 8000 (20 to 25% 0·1 M-cacodylate buffer (pH 6·5) and 1% 2-mehtyl-2,4-pentanediol. Oxidation of the protein is critical for reproducibly obtaining high quality crystals. The resulting crystals diffract to 2 Å and belong to the monoclinic space group C 2 with cel dimensions a=117·5 Å, b =65·0 Å, c76·3 Å, β=126·3° with two molecules in the asymmetric unit.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom1097
dc.relation.ispartofpageto1100
dc.relation.ispartofissue3
dc.relation.ispartofjournalJournal of Molecular Biology
dc.relation.ispartofvolume230
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode3107
dc.titleCrystallization of DsbA, an Escherichia coli Protein Required for Disulphide Bond Formation in Vivo
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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