The status of the macromolecular crystallography beamlines at the European Synchrotron Radiation Facility

The European Synchrotron Radiation Facility (ESRF) is the oldest and most powerful 3rd generation synchrotron in Europe, providing X-rays to more than 40 experimental stations welcoming several thousand researchers per year. A major success story has been the ESRF's facilities for macromolecular crystallography (MX). These are grouped around 3 straight sections: On ID23 canted undulators accommodate ID23-1, a mini-focus tuneable energy end station and ID23-2, the world's first micro-focus beamline dedicated to MX; ID29 houses a single, mini-focus, tuneable energy end station; ID30 will provide three end stations for MX due in operation from mid-2014 to early 2015. Here, one branch of a canted X-ray source feeds two fixed-energy end stations (MASSIF-1, MASSIF-3). The second feeds ID30B, a variable focus, tuneable energy beamline. MASSIF-1 is optimised for automatic high-throughput experiments requiring a relatively large beam size at the sample position, MASSIF-3 is a high-intensity, micro-focus facility designed to complement ID23-2. All end stations are highly automated, equipped with sample mounting robots and large area, fast-readout photon-counting detectors. Experiment control and tracking is achieved via a combination of the MXCuBE2 graphical user interface and the ISPyB database, the former allowing user-friendly control of all beamline components, the latter providing data tracking before, after and during experiments.

[1]  Randy J. Read,et al.  Acta Crystallographica Section D Biological , 2003 .

[2]  F Cipriani,et al.  Automation of sample mounting for macromolecular crystallography. , 2006, Acta crystallographica. Section D, Biological crystallography.

[3]  Didier Nurizzo,et al.  Recent progress in robot-based systems for crystallography and their contribution to drug discovery , 2013, Expert opinion on drug discovery.

[4]  Florent Cipriani,et al.  Inducing phase changes in crystals of macromolecules: status and perspectives for controlled crystal dehydration. , 2011, Journal of structural biology.

[5]  Frank Schluenzen,et al.  High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium , 2001, Cell.

[6]  V. Ramakrishnan,et al.  Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics , 2000, Nature.

[7]  Christoph Mueller-Dieckmann,et al.  In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF , 2015, Acta crystallographica. Section D, Biological crystallography.

[8]  E. Pebay-Peyroula,et al.  X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. , 1997, Science.

[9]  Owen Johnson,et al.  iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM , 2011, Acta crystallographica. Section D, Biological crystallography.

[10]  D. Svergun,et al.  BioSAXS Sample Changer: a robotic sample changer for rapid and reliable high-throughput X-ray solution scattering experiments , 2015, Acta crystallographica. Section D, Biological crystallography.

[11]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..

[12]  Didier Nurizzo,et al.  A decade of user operation on the macromolecular crystallography MAD beamline ID14-4 at the ESRF , 2009, Journal of synchrotron radiation.

[13]  Sebastien Petitdemange,et al.  Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collection. , 2010, Acta crystallographica. Section D, Biological crystallography.

[14]  Florent Cipriani,et al.  Improving diffraction by humidity control: a novel device compatible with X-ray beamlines. , 2009, Acta crystallographica. Section D, Biological crystallography.

[15]  Olof Svensson,et al.  The use of workflows in the design and implementation of complex experiments in macromolecular crystallography , 2012, Acta crystallographica. Section D, Biological crystallography.

[16]  Didier Nurizzo,et al.  Online collection and analysis of X-ray fluorescence spectra on the macromolecular crystallography beamlines of the ESRF , 2009 .

[17]  A. N. Popov,et al.  Optimization of data collection taking radiation damage into account , 2010, Acta crystallographica. Section D, Biological crystallography.

[18]  M. Bowler,et al.  Measurement of the intrinsic variability within protein crystals: implications for sample-evaluation and data-collection strategies. , 2014, Acta crystallographica. Section F, Structural biology communications.

[19]  Christian Morawe,et al.  The ID23-2 structural biology microfocus beamline at the ESRF , 2009, Journal of synchrotron radiation.

[20]  P Theveneau,et al.  ID14 'Quadriga', a Beamline for Protein Crystallography at the ESRF. , 1998, Journal of synchrotron radiation.

[21]  Adam Round,et al.  Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography. , 2013, Acta crystallographica. Section D, Biological crystallography.

[22]  Segmenting data sets for RIP. , 2012, Acta crystallographica. Section D, Biological crystallography.

[23]  Adam Round,et al.  ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments , 2015, Acta crystallographica. Section D, Biological crystallography.

[24]  Christoph Mueller-Dieckmann,et al.  Towards a high-throughput system for high-pressure cooling of cryoprotectant-free biological crystals , 2014 .

[25]  Didier Nurizzo,et al.  The ID23-1 structural biology beamline at the ESRF. , 2006, Journal of synchrotron radiation.

[26]  F Cipriani,et al.  Protein microcrystals and the design of a microdiffractometer: current experience and plans at EMBL and ESRF/ID13. , 1999, Acta crystallographica. Section D, Biological crystallography.

[27]  Armin Wagner,et al.  Protein crystallography with a novel large-area pixel detector , 2006 .

[28]  Randy J. Read,et al.  Overview of the CCP4 suite and current developments , 2011, Acta crystallographica. Section D, Biological crystallography.

[29]  Olof Svensson,et al.  ISPyB: an information management system for synchrotron macromolecular crystallography , 2011, Bioinform..

[30]  Stéphanie Malbet-Monaco,et al.  How the ESRF helps industry and how they help the ESRF , 2013, Acta crystallographica. Section D, Biological crystallography.

[31]  R. Ravelli,et al.  The use of a mini-κ goniometer head in macromolecular crystallography diffraction experiments , 2013, Acta crystallographica. Section D, Biological crystallography.

[32]  Anton Barty,et al.  Room-temperature macromolecular serial crystallography using synchrotron radiation , 2014, IUCrJ.

[33]  C. Vonrhein,et al.  Structure of the 30S ribosomal subunit , 2000, Nature.

[34]  Gordon A Leonard,et al.  ID29: a high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering. , 2012, Journal of synchrotron radiation.

[35]  Dan S. Tawfik,et al.  The molecular basis of phosphate discrimination in arsenate-rich environments , 2012, Nature.

[36]  C. Spahn,et al.  The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre , 2011, Nature.

[37]  E. Tajkhorshid,et al.  Subangstrom Resolution X-Ray Structure Details Aquaporin-Water Interactions , 2013, Science.

[38]  T. Richmond,et al.  Crystal structure of the nucleosome core particle at 2.8 Å resolution , 1997, Nature.

[39]  Henry N. Chapman,et al.  Serial crystallography on in vivo grown microcrystals using synchrotron radiation , 2014, IUCrJ.

[40]  Janet L. Smith.  Determination of three-dimensional structure by multiwavelength anomalous diffraction: Current Opinion in Structural Biology 1991, 1:1002–1011 , 1991 .

[41]  Didier Nurizzo,et al.  MxCuBE: a synchrotron beamline control environment customized for macromolecular crystallography experiments , 2010, Journal of synchrotron radiation.

[42]  Wayne A Hendrickson,et al.  [28] Phase determination from multiwavelength anomalous diffraction measurements. , 1997, Methods in enzymology.

[43]  Kevan M. Shokat,et al.  Structures of PI4KIIIβ complexes show simultaneous recruitment of Rab11 and its effectors , 2014, Science.

[44]  Didier Nurizzo,et al.  The Upgrade Programme for the Structural Biology beamlines at the European Synchrotron Radiation Facility – High throughput sample evaluation and automation , 2013 .

[45]  Gebhard F. X. Schertler,et al.  Structure of a β1-adrenergic G-protein-coupled receptor , 2008, Nature.

[46]  C. Mueller-Dieckmann,et al.  Upgraded ESRF BM29 beamline for SAXS on macromolecules in solution , 2013, Journal of synchrotron radiation.

[47]  S. Brockhauser,et al.  Automation and Experience of Controlled Crystal Dehydration: Results from the European Synchrotron HC1 Collaboration , 2015 .

[48]  Nathan Nelson,et al.  Structure Determination and Improved Model of Plant Photosystem I* , 2009, The Journal of Biological Chemistry.

[49]  Olof Svensson,et al.  Automatic processing of macromolecular crystallography X-ray diffraction data at the ESRF , 2013, Journal of applied crystallography.

[50]  M. Burghammer,et al.  Crystal structure of the human β2 adrenergic G-protein-coupled receptor , 2007, Nature.

[51]  Didier Nurizzo,et al.  An inexpensive automatically operated device for the flash annealing of crystals of macromolecules , 2009 .

[52]  H Toyokawa,et al.  The PILATUS 1M detector. , 2006, Journal of synchrotron radiation.

[53]  W. Hunter,et al.  De novo phasing of two crystal forms of tryparedoxin II using the anomalous scattering from S atoms: a combination of small signal and medium resolution reveals this to be a general tool for solving protein crystal structures. , 2002, Acta crystallographica. Section D, Biological crystallography.

[54]  A. N. Popov,et al.  The application of hierarchical cluster analysis to the selection of isomorphous crystals. , 2012, Acta Crystallographica Section D: Biological Crystallography.

[55]  G. Sheldrick.  A short history of SHELX. , 2008, Acta crystallographica. Section A, Foundations of crystallography.

[56]  R. Ravelli,et al.  Phasing in the presence of radiation damage , 2005 .

[57]  Gordon A Leonard,et al.  Automatic structure determination based on the single-wavelength anomalous diffraction technique away from an absorption edge. , 2005, Acta crystallographica. Section D, Biological crystallography.

[58]  John M. Berrisford,et al.  Crystal structure of the entire respiratory complex I , 2013, Nature.

[59]  H. Hope.  Cryocrystallography of biological macromolecules: a generally applicable method. , 1988, Acta crystallographica. Section B, Structural science.