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dc.contributor.authorBrown, J.en_US
dc.contributor.authorWalter, T.en_US
dc.contributor.authorCarter, L.en_US
dc.contributor.authorAbrescia, N. A.en_US
dc.contributor.authorAricescu, A.en_US
dc.contributor.authorBatuwangala, T.en_US
dc.contributor.authorBird, L.en_US
dc.contributor.authorBrown, N.en_US
dc.contributor.authorChamberlain, P.en_US
dc.contributor.authorDavis, S.en_US
dc.contributor.authorDubinina, E.en_US
dc.contributor.authorEndicott, J.en_US
dc.contributor.authorFennelly, J.en_US
dc.contributor.authorGilbert, R. C.en_US
dc.contributor.authorHarkiolaki, M.en_US
dc.contributor.authorHon, W.en_US
dc.contributor.authorKimberley, F.en_US
dc.contributor.authorLove, C.en_US
dc.contributor.authorMancini, E.en_US
dc.contributor.authorManso-Sancho, R.en_US
dc.contributor.authorNichols, C.en_US
dc.contributor.authorRobinson, R.en_US
dc.contributor.authorSutton, G.en_US
dc.contributor.authorSchueller, N.en_US
dc.contributor.authorSleeman, M.en_US
dc.contributor.authorStewart-Jones, G.en_US
dc.contributor.authorVuong, M.en_US
dc.contributor.authorWelburn, J.en_US
dc.contributor.authorZhang, Z.en_US
dc.contributor.authorStammers, D.en_US
dc.contributor.authorOwens, R.en_US
dc.contributor.authorJones, E.en_US
dc.contributor.authorHarlos, K.en_US
dc.contributor.authorStuart, D.en_US
dc.description.abstractAn initial tranche of results from day-to-day use of a robotic system for setting up 100 nl-scale vapour-diffusion sitting-drop protein crystallizations has been surveyed. The database of over 50 unrelated samples represents a snapshot of projects currently at the stage of crystallization trials in Oxford research groups and as such encompasses a broad range of proteins. The results indicate that the nanolitre-scale methodology consistently identifies more crystallization conditions than traditional hand-pipetting-style methods; however, in a number of cases successful scale-up is then problematic. Crystals grown in the initial 100 nl-scale drops have in the majority of cases allowed useful characterization of X-ray diffraction, either in-house or at synchrotron beamlines. For a significant number of projects, full X-ray diffraction data sets have been collected to 3 Šresolution or better (either in-house or at the synchrotron) from crystals grown at the 100 nl scale. To date, five structures have been determined by molecular replacement directly from such data and a further three from scale-up of conditions established at the nanolitre scale.en_US
dc.publisherWiley-Blackwell Munksgaarden_US
dc.relation.ispartofjournalJournal of Applied Crystallographyen_US
dc.titleA procedure for setting up high-throughput nanolitre crystallization experiments. II. Crystallization resultsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyright© 2003 Blackwell Munksgaard and the author[s]. The definitive version is available at www.interscience.wiley.comen_US
gro.hasfulltextNo Full Text

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