European Molecular Biology Laboratory 4 articles published in JoVE Biochemistry The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble Irina Cornaciu1,2, Raphael Bourgeas1, Guillaume Hoffmann1, Florine Dupeux1,3, Anne-Sophie Humm1, Vincent Mariaule1, Andrea Pica1,2, Damien Clavel1,2, Gael Seroul1,2, Peter Murphy1, José Antonio Márquez1,2 1European Molecular Biology Laboratory, 2ALPX S.A.S., 3Institut de Biologie Structurale Here, we describe how to use the automated macromolecular crystallography pipelines for protein-to-structure, rapid ligand-protein complex analysis and large-scale fragment screening based on the CrystalDirect technology at the HTX Laboratory in EMBL Grenoble. Biochemistry Fixed Target Serial Data Collection at Diamond Light Source Sam Horrell1, Danny Axford1, Nicholas E. Devenish1, Ali Ebrahim1, Michael A. Hough2, Darren A. Sherrell1,3, Selina L. S. Storm1,4, Ivo Tews5, Jonathan A. R. Worrall2, Robin L. Owen1 1Diamond Light Source, Harwell Science and Innovation Campus, 2School of Life Sciences, University of Essex, 3X-ray Science Division, Argonne National Laboratory, 4European Molecular Biology Laboratory, Hamburg Outstation c/o DESY, 5Biological Sciences, Institute for Life Sciences, University of Southampton We present a comprehensive guide to fixed target sample preparation, data collection, and data processing for serial synchrotron crystallography at Diamond beamline I24. Biochemistry Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules Stephanie Hutin1, Bart Van Laer1, Christoph Mueller-Dieckmann1, Gordon Leonard1, Didier Nurizzo1, Matthew W. Bowler2 1Structural Biology Group, European Synchrotron Radiation Facility, 2Grenoble Outstation, European Molecular Biology Laboratory Here, we describe how to use the automated screening and data collection options available at some synchrotron beamlines. Scientists send cryocooled samples to the synchrotron, and the diffraction properties are screened, the data sets are collected and processed and, where possible, a structure solution is carried out—all without human intervention. Biochemistry Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect Stephanie Hutin*1, Gianluca Santoni*1, Ulrich Zander2, Nicolas Foos1, Sylvain Aumonier1, Guillaume Gotthard1, Antoine Royant1,3, Christoph Mueller-Dieckmann1, Gordon Leonard1 1European Synchrotron Radiation Facility, Structural Biology Group, 2European Molecular Biology Laboratory, 3Univ. Grenoble Alpes, CNRS, CEA, IBS (Institut de Biologie Structurale) We present the use of the MeshAndCollect protocol to obtain a complete diffraction data set, for use in subsequent structure determination, composed of partial diffraction data sets collected from many small crystals of the fluorescent protein Cerulean.
