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      Online data analysis at the ESRF bioSAXS beamline, BM29

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          Abstract

          High-throughput small-angle X-ray scattering on proteins in solution (bioSAXS) at synchrotron sources is a commonly used technique in structural biology, which relies on highly automated data acquisition. Data reduction and primary analysis for bioSAXS experiments consist of a well defined series of individual tasks, the automation of which allows a first easy assessment of the quality of collected data and the adjustment of collection strategies if necessary. This article describes both the logic and the technical implementation of the automated processing pipeline for bioSAXS data at the ESRF BM29 beamline using theEDNAframework.

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          Python for Scientific Computing

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            Cython: The Best of Both Worlds

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              Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)

              We present an efficient pipeline enabling high-throughput analysis of protein structure in solution with small angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling of microliter volumes, temperature and anaerobic control, rapid data collection, data analysis, and couples structural analysis with automated archiving. We subjected 50 representative proteins, mostly from Pyrococcus furiosus, to this pipeline, revealing that 30 were multimeric structures in solution. SAXS analysis allowed us to distinguish aggregated and unfolded proteins, define global structural parameters and oligomeric states for most samples, identify shapes and similar structures for 25 unknown structures, and determine envelopes for 41 proteins. We believe that high throughput SAXS is an enabling technology that may change the way that structural genomics research is done.
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                Author and article information

                Journal
                JACGAR
                Journal of Applied Crystallography
                J Appl Crystallogr
                International Union of Crystallography (IUCr)
                1600-5767
                February 2016
                February 2016
                : 49
                : 1
                : 203-212
                Article
                10.1107/S1600576715024462
                a96a8d8f-29cf-4785-af57-3eee9f19d9d4
                © 2016
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