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Brown, J; Walter, T S; Carter, L; Abrescia, N G A; Aricescu, A R; Batuwangala, T D; Bird, L E; Brown, N; Chamberlain, P P; Davis, S J; Dubinina, E; Endicott, J; Fennelly, J A; Gilbert, R J C; Harkiolaki, M; Hon, W-C; Kimberley, F; Love, C A; Mancini, E J; Manso-Sancho, R; Nichols, C E; Robinson, R A; Sutton, G C; Schueller, N; Sleeman, M C; Stewart-Jones, G B; Vuong, M; Welburn, J; Zhang, Z; Stammers, D K ... view all 34 authors View less authors (2003)
Publisher: International Union of Crystallography
Languages: English
Types: Article
Subjects: Q
An 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 Å resolution 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.
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