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dc.contributor.authorBrown, J
dc.contributor.authorWalter, TS
dc.contributor.authorCarter, L
dc.contributor.authorAbrescia, NGA
dc.contributor.authorAricescu, AR
dc.contributor.authorBatuwangala, TD
dc.contributor.authorBird, LE
dc.contributor.authorBrown, N
dc.contributor.authorChamberlain, PP
dc.contributor.authorDavis, SJ
dc.contributor.authorDubinina, E
dc.contributor.authorEndicott, J
dc.contributor.authorFennelly, JA
dc.contributor.authorGilbert, RJC
dc.contributor.authorHarkiolaki, M
dc.contributor.authorHon, WC
dc.contributor.authorKimberley, F
dc.contributor.authorLove, CA
dc.contributor.authorMancini, EJ
dc.contributor.authorManso-Sancho, R
dc.contributor.authorNichols, CE
dc.contributor.authorRobinson, RA
dc.contributor.authorSutton, GC
dc.contributor.authorSchueller, N
dc.contributor.authorSleeman, MC
dc.contributor.authorStewart-Jones, GB
dc.contributor.authorVuong, M
dc.contributor.authorWelburn, J
dc.contributor.authorZhang, Z
dc.contributor.authorStammers, DK
dc.contributor.authorOwens, RJ
dc.contributor.authorJones, EY
dc.contributor.authorHarlos, K
dc.contributor.authorStuart, DI
dc.date.accessioned2017-05-03T11:37:24Z
dc.date.available2017-05-03T11:37:24Z
dc.date.issued2003
dc.date.modified2009-09-03T07:17:52Z
dc.identifier.issn0021-8898
dc.identifier.doi10.1107/S0021889803002012
dc.identifier.urihttp://hdl.handle.net/10072/22002
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_AU
dc.publisherWiley-Blackwell Munksgaard
dc.publisher.placeDenmark
dc.publisher.urihttp://www.wiley.com/bw/journal.asp?ref=0021-8898
dc.relation.ispartofpagefrom315
dc.relation.ispartofpageto318
dc.relation.ispartofissue2
dc.relation.ispartofjournalJournal of Applied Crystallography
dc.relation.ispartofvolume36
dc.subject.fieldofresearchMathematical Sciences
dc.subject.fieldofresearchPhysical Sciences
dc.subject.fieldofresearchEngineering
dc.subject.fieldofresearchcode01
dc.subject.fieldofresearchcode02
dc.subject.fieldofresearchcode09
dc.titleA procedure for setting up high-throughput nanolitre crystallization experiments. II. Crystallization results
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2003 Blackwell Munksgaard and the author[s]. The definitive version is available at www.interscience.wiley.com
gro.date.issued2003
gro.hasfulltextNo Full Text
gro.griffith.authorLove, Christopher A.


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