1. Research
  2. Collaborations
  3. Publications
  4. Group
Research -

Current Research Interests

My research group at Diamond is focused on three areas of development:

  1. Development of core software and algorithms for Macromolecular Crystallography such as DIALS, BLEND and CHOOCH.
  2. Development of automated pipelines and tools to enable their implementation
  3. Developement of instrumentation and methods for X-ray diffraction beamlines including sample preparation and mounting

Projects

DIALS

I lead the DIALS project for the development of new integration software to capitailise on new detector technology and push the boundaries in terms of the quality of diffraction data that can be integrated and the quality of samples that can be addressed. We are funded by Diamond, the EU BioStruct-X grant and CCP4. We collaborate with Andrew Leslie, Phil Evans and Garib Murshudov from the MRC Laboratory of Molecular Biology in Cambridge, with Gleb Bourenkov from EMBL in Hamburg and with the group of Nick Sauter at the Berkley Laboratory, USA. DIALS is currently available as a pre-release test or development version from dials.diamond.ac.uk.

DIALS group at Diamond

  • Graeme Winter (Diamond)
  • David Waterman (CCP4)
  • James Parkhurst (BioStruct-X/Diamond)
  • Luis Fuentes-Montero (BioStruct-X/Diamond)
  • Richard Gildea (Diamond)

Blend

The development of software for the determination of optimal data subsets from partial multicrystal data sets (BLEND). BLEND sits between the data integration and scaling stages and allows users to conveniently collate large numbers of data sets and, based on cell dimension cluster analysis, group these data sets into likely isomorphous groups in preparation for scaling. BLEND will then use Pointless and Aimless (from CCP4) to automatically scale each group and output a plot of Rmeas vs. completeness for all scaled groups.

X-Ray Tomography and Radiography

The development of X-ray microtomographic techniques for MX which can be used to align and characterise crystals embedded in otherwise opaque materials.

Dynamic X-ray microapertures

Development of microapertures for the precise definition of microbeams on MX beamlines.

 

Collaborations - +

Collaborations

DIALS

Our key collaborators in the DIALS project are Nick Sauter (from LBNL, Berkley, CA) and CCP4. We are also gretaly indebted for continued enthusiasm and expert input from collaborators at the MRC-LMB in Cambridge, Andrew Leslie, Harry Powell, Phil Evans and Garib Murshudov.

CCP4

I have worked closely with CCP4 for many years and am currently a member of their Executive Committee. DIALS form part of a major collabroation with CCP4 and from late 2015 it will be released as part of the CCP4 program suite. CHOOCH and BLEND are alraedy distributed by CCP4. In December 2014 Diamond and CCP4 launched the jointly funded Diamond-CCP4 Data Collection and Analysis course and this course will now run yearly with an aim to continue best practice teaching in these core macromolecular crystallography skills.

Membrane Protein Laboratory (MPL) at Diamond

In 2007 the Diamond MPL was launched with funding from the Wellcome Trust. The project was led by Prof. So Iwata and Prof. Dame Louise Johnson, with Gwyndaf Evans making contributions to methods development and forming a valuable link with the I24 microfocus beamline at Diamond.

The MPL is operated principally as a user facility and since its launch has nurtured over 40 membrane protein projects from the UK and abroad. An introduction to the MPL can be seen here.

The lab is managed on a daily basis by Dr Isabel de Moraes who also sits in the MPL management committe with Prof So Iwata, Prof Dave Stuart and Dr Evans.

The MPL has recently received funding for a further 3 years from 2013, and we continue to welcome interest from researchers wanting to progress their membrane proteins through purification, crystallization and ultimately data collection at Diamond.

Publications - +

Publications

  • Laundy, D., Alianelli, L., Sutter, J., Evans, G. & Sawhney, K. Surface profiling of X-ray mirrors for shaping focused beams. Optics Express 23, 1576-1584 (2015).
  • Aller, P. et al. Application of In Situ Diffraction in High-Throughput Structure Determination Platforms. in Structural Proteomics Vol. 1261 Methods in Molecular Biology (ed Raymond J. Owens) Ch. 13, 233-253 (Springer New York, 2014).
  • Parkhurst, J. M. et al. dxtbx: the diffraction experiment toolbox. Journal of Applied Crystallography 47, 1459-1465, doi:doi:10.1107/S1600576714011996 (2014).
  • Owen, R. L. et al. Exploiting fast detectors to enter a new dimension in room-temperature crystallography. Acta Crystallographica Section D 70, 1248-1256, doi:doi:10.1107/S1399004714005379 (2014).
  • Moraes, I., Evans, G., Sanchez-Weatherby, J., Newstead, S. & Stewart, P. D. S. Membrane protein structure determination — The next generation. Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, 78-87, doi:http://dx.doi.org/10.1016/j.bbamem.2013.07.010 (2014).
  • Gildea, R. J. et al. New methods for indexing multi-lattice diffraction data. Acta Crystallographica Section D 70, 2652-2666, doi:doi:10.1107/S1399004714017039 (2014).
  • Warren, A. J. et al. Visualization of membrane protein crystals in lipid cubic phase using X-ray imaging. Acta Crystallographica Section D 69, 1252-1259, doi:doi:10.1107/S0907444913011359 (2013).
  • Paterno, G. et al. Micro-focused X-ray diffraction characterization of high-quality [6,6]-phenyl-C61-butyric acid methyl ester single crystals without solvent impurities. Journal of Materials Chemistry C, doi:10.1039/C3TC31075B (2013).
  • Foadi, J. et al. Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography. Acta Crystallographica Section D 69, 1617-1632 (2013).
  • Wang, X. et al. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat Struct Mol Biol 19, 424-429, doi:http://www.nature.com/nsmb/journal/v19/n4/abs/nsmb.2255.html#supplementary-information (2012).
  • Ramraj, V., Evans, G., Diprose, J. M. & Esnouf, R. M. Nearest-cell: a fast and easy tool for locating crystal matches in the PDB. Acta Crystallographica Section D 68, 1697-1700, doi:doi:10.1107/S0907444912040590 (2012).
  • Owen, R. L. et al. Outrunning free radicals in room-temperature macromolecular crystallography. Acta Crystallographica Section D 68, 810-818 (2012).
  • Gessmann, R., Axford, D., Evans, G., Brückner, H. & Petratos, K. The crystal structure of samarosporin I at atomic resolution. Journal of Peptide Science 18, 678-684 (2012).
  • Axford, D. et al. In situ macromolecular crystallography using microbeams. Acta Crystallographica Section D 68, 592-600 (2012).
  • Merrifield, D. R. et al. A novel technique combining high-resolution synchrotron x-ray microtomography and x-ray diffraction for characterization of micro particulates. Measurement Science and Technology 22, 115703 (2011).
  • Foadi, J. & Evans, G. On the allowed values for the triclinic unit-cell angles. Acta Crystallographica Section A 67, 93-95, doi:doi:10.1107/S0108767310044296 (2011).
  • Evans, G., Axford, D., Waterman, D. & Owen, R. L. Macromolecular microcrystallography. Crystallography Reviews 17, 105 - 142 (2011).
  • Evans, G., Axford, D. & Owen, R. L. The design of macromolecular crystallography diffraction experiments. Acta Cryst. D 67, 261-270, doi:doi:10.1107/S0907444911007608 (2011).
  • Waterman, D. & Evans, G. Estimation of errors in diffraction data measured by CCD area detectors. Journal of Applied Crystallography 43, 1356-1371, doi:doi:10.1107/S0021889810033418 (2010).
  • Ji, X. et al. How baculovirus polyhedra fit square pegs into round holes to robustly package viruses. EMBO Journal. 29, 505-514 (2010). Hausmann, J. et al. Mammalian cell expression, purification, crystallization and microcrystal data collection of autotaxin/ENPP2, a secreted mammalian glycoprotein. Acta Cryst. F 66, 1130-1135, doi:doi:10.1107/S1744309110032938 (2010).
  • Aishima, J. et al. High-speed crystal detection and characterization using a fast-readout detector. Acta Cryst. D 66, 1032-1035, doi:10.1107/s0907444910028192 (2010).
  • Foadi, J. & Evans, G. Elucidations on the reciprocal lattice and the Ewald sphere. European Journal of Physics 29, 1059-1068, doi:10.1088/0143-0807/29/5/017 (2008).
  • Evans, G., Alianelli, L., Burt, M., Wagner, A. & Sawhney, K. J. S. Diamond Beamline I24: A Flexible Instrument for Macromolecular Micro-crystallography. AIP Conference Proceedings 879, 836-839 (2007).
  • Rosenbaum, G. et al. The Structural Biology Center 19ID undulator beamline: facility specifications and protein crystallographic results. Journal of Synchrotron Radiation 13, 30-45, doi:doi:10.1107/S0909049505036721 (2006).
  • Poole, K. J. V. et al. A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle. Journal of Structural Biology 155, 273-284, doi:10.1016/j.jsb.2006.02.020 (2006).
  • Izard, T. et al. Vinculin activation by talin through helical bundle conversion. Nature 427, 171-175, doi:10.1038/nature02281 (2004).
  • Evans, G., Polentarutti, M., Carugo, K. D. & Bricogne, G. SAD phasing with triiodide, softer X-rays and some help from radiation damage. Acta Crystallographica Section D-Biological Crystallography 59, 1429-1434 (2003).
  • Evans, G. & Bricogne, G. Triiodide derivatization in protein crystallography. Acta Crystallographica Section D-Biological Crystallography 59, 1923-1929, doi:10.1107/s0907444903012897 (2003).
  • Evans, G. & Bricogne, G. Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu K alpha X-ray equipment. Acta Crystallographica Section D-Biological Crystallography 58, 976-991, doi:10.1107/s0907444902005486 (2002).
  • Evans, G. & Pettifer, R. F. CHOOCH: a program for deriving anomalous-scattering factors from X-ray fluorescence spectra. Journal of Applied Crystallography 34, 82-86 (2001).
  • Roversi, P., Blanc, E., Vonrhein, C., Evans, G. & Bricogne, G. Modelling prior distributions of atoms for macromolecular refinement and completion. Acta Crystallographica Section D-Biological Crystallography 56, 1316-1323 (2000).
  • Evans, G., Roversi, P. & Bricogne, G. In-house low-resolution X-ray crystallography. Acta Crystallographica Section D-Biological Crystallography 56, 1304-1311 (2000).
  • Alkire, R. W., Rosenbaum, G. & Evans, G. Design of a vacuum-compatible high-precision monochromatic beam-position monitor for use with synchrotron radiation from 5 to 25 keV. J. Synchrotron Rad. 7, 61-68 (2000).
  • Zhang, R. G. et al. Characteristics and crystal structure of bacterial inosine-5 '-monophosphate dehydrogenase. Biochemistry 38, 4691-4700 (1999).
  • Zhang, R. G. et al. Differential signatures of bacterial and mammalian IMP dehydrogenase enzymes. Current Medicinal Chemistry 6, 537-543 (1999).
  • Walsh, M. A., Evans, G., Sanishvili, R., Dementieva, I. & Joachimiak, A. MAD data collection - current trends. Acta Crystallographica Section D-Biological Crystallography 55, 1726-1732 (1999).
  • Walsh, M. A., Dementieva, I., Evans, G., Sanishvili, R. & Joachimiak, A. Taking MAD to the extreme: ultrafast protein structure determination. Acta Crystallographica Section D-Biological Crystallography 55, 1168-1173 (1999).
  • Evans, G. & Wilson, K. S. A MAD experiment performed at the white line of the iridium L-III absorption edge in lysozyme. Acta Crystallographica Section D-Biological Crystallography 55, 67-76 (1999).
  • Evans, G. & Pettifer, R. F. Stabilization and calibration of x-ray wavelengths for anomalous diffraction measurements using synchrotron radiation. Review of Scientific Instruments 67, 3428-3433 (1996).

 

Group - +

Staff and PDRAs

  • Jose Trincao
  • Pierre Aller
  • Anna Warren
  • James Parkhurst
  • Luis Fuentes-Montero
  • Richard Gildea
  • Melanie Vollmar

PhD Students

  • Matt Rodriguez (University of Southampton with Dr Ivo Tews)

Past PhD Students

  • Varun Ramraj (University of Oxford with Robert Esnouf)
  • Siti Nurul'Ain Yusop (University of Leeds with Prof. Kevin Roberts)

 

Gwyndaf Evans

profilephoto

Gwyndaf Evans is Principal Beamline Scientist for VMXm and a Diamond Research Fellow.

 

Email: gwyndaf.evans@diamond.ac.uk
Tel: +44 (0) 1235 778164

Key Research Area

Key Research Area

  • Software development for MX
  • X-ray instrumentation
  • Methods development

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