Dear BB-members, The January issue of Acta Cryst section D features the proceedings of the Study Weekend 2014 on Complementary Methods, contains 16 articles, and is available online (open access) at http://journals.iucr.org/d/issues/2015/01/00/issconts.html
A happy 2015, and c u @ the 2015 study weekend! Ivo Tews Macromolecular Crystallography – CCP4 WG2 chair – Natural Sciences Admissions University of Southampton, Centre for Biological Sciences Institute for Life Sciences (IfLS) B85, Highfield Campus Southampton SO17 1BJ phone: ++44 (0)23-8059-4415 lab: -4365 fax: -5159 mobile: ++44(0)752-775-7696 http://www.soton.ac.uk/sdc http://www.researcherid.com/rid/A-2750-2010 http://www.southampton.ac.uk/biosci/about/staff/it1y09.page? Acta Crystallographica Section D Biological Crystallography Volume 71, Part 1 (January 2015) ________________________________ Crystallography and complementary methods Proceedings of the CCP4<http://www.ccp4.ac.uk/> study weekend [[Issue Author Index]]<http://journals.iucr.org/d/issues/2015/01/00/saindx.html>[[Volume Author Index]]<http://journals.iucr.org/d/issues/2015/csaindx.html> [[Cover illustration]] Cover illustration: Crystallography and complementary methods. * introduction<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#introduction1> * biophysics<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#biophysics2> * SAXS<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#SAXS3> * new mounts<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#new_mounts4> * EM<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#EM5> * dynamics<http://journals.iucr.org/d/issues/2015/01/00/isscontsbdy.html#dynamics6> ________________________________ introduction ________________________________ [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5230/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5230/ba5230.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 1-2 [ doi:10.1107/S1399004714027321<http://dx.doi.org/10.1107/S1399004714027321> ] Two way street - complementary methods I. Tews<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Tews%2C%20I%2E> and J. Cooper<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Cooper%2C%20J%2E> Synopsis: An introduction to the 2014 CCP4 Study Weekend. Online 1 January 2015 ________________________________ biophysics ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5223/ba5223bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5223/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5223/ba5223.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 3-14 [ doi:10.1107/S1399004714010372<http://dx.doi.org/10.1107/S1399004714010372> ] Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT H. Zhao<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Zhao%2C%20H%2E> and P. Schuck<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Schuck%2C%20P%2E> Synopsis: Global multi-method analysis for protein interactions (GMMA) can increase the precision and complexity of binding studies for the determination of the stoichiometry, affinity and cooperativity of multi-site interactions. The principles and recent developments of biophysical solution methods implemented for GMMA in the software SEDPHAT are reviewed, their complementarity in GMMA is described and a new GMMA simulation tool set in SEDPHAT is presented. Online 11 December 2014 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5220/ba5220bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5220/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5220/ba5220.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 15-26 [ doi:10.1107/S139900471401517X<http://dx.doi.org/10.1107/S139900471401517X> ] In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF D. von Stetten<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=von%20Stetten%2C%20D%2E>, T. Giraud<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Giraud%2C%20T%2E>, P. Carpentier<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Carpentier%2C%20P%2E>, F. Sever<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Sever%2C%20F%2E>, M. Terrien<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Terrien%2C%20M%2E>, F. Dobias<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Dobias%2C%20F%2E>, D. H. Juers<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Juers%2C%20D%2EH%2E>, D. Flot<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Flot%2C%20D%2E>, C. Mueller-Dieckmann<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Mueller%2DDieckmann%2C%20C%2E>, G. A. Leonard<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Leonard%2C%20G%2EA%2E>, D. de Sanctis<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=de%20Sanctis%2C%20D%2E> and A. Royant<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Royant%2C%20A%2E> Synopsis: The current version of the Cryobench in crystallo optical spectroscopy facility of the ESRF is presented. The diverse experiments that can be performed at the Cryobench are also reviewed. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5221/ba5221bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5221/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5221/ba5221.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/ba5221/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 27-35 [ doi:10.1107/S1399004714015107<http://dx.doi.org/10.1107/S1399004714015107> ] Challenges and solutions for the analysis of in situ, in crystallo micro-spectrophotometric data F. S. N. Dworkowski<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Dworkowski%2C%20F%2ES%2EN%2E>, M. A. Hough<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Hough%2C%20M%2EA%2E>, G. Pompidor<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pompidor%2C%20G%2E> and M. R. Fuchs<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Fuchs%2C%20M%2ER%2E> Synopsis: The particular challenge of the analysis of optical absorption and Raman spectroscopic data measured from protein crystals and how the SLS-APEsoftware toolbox supports scientists in dealing with such data is described. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5217/ba5217bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5217/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5217/ba5217.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/ba5217/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 36-44 [ doi:10.1107/S1399004714016617<http://dx.doi.org/10.1107/S1399004714016617> ] Protein-ligand interactions investigated by thermal shift assays (TSA) and dual polarization interferometry (DPI) M. K. Grøftehauge<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gr%26oslash%3Bftehauge%2C%20M%2EK%2E>, N. R. Hajizadeh<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Hajizadeh%2C%20N%2ER%2E>, M. J. Swann<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Swann%2C%20M%2EJ%2E> and E. Pohl<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pohl%2C%20E%2E> Synopsis: The biophysical characterization of protein-ligand interactions in solution using techniques such as thermal shift assay, or on surfaces using, for example, dual polarization interferometry, plays an increasingly important role in complementing crystal structure determinations. Online 1 January 2015 ________________________________ SAXS ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/mn5059/mn5059bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/mn5059/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/mn5059/mn5059.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/mn5059/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 45-56 [ doi:10.1107/S1399004714010876<http://dx.doi.org/10.1107/S1399004714010876> ] The accurate assessment of small-angle X-ray scattering data T. D. Grant<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Grant%2C%20T%2ED%2E>, J. R. Luft<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Luft%2C%20J%2ER%2E>, L. G. Carter<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Carter%2C%20L%2EG%2E>, T. Matsui<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Matsui%2C%20T%2E>, T. M. Weiss<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Weiss%2C%20T%2EM%2E>, A. Martel<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Martel%2C%20A%2E> and E. H. Snell<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Snell%2C%20E%2EH%2E> Synopsis: A set of quantitative techniques is suggested for assessing SAXS data quality. These are applied in the form of a script, SAXStats, to a test set of 27 proteins, showing that these techniques are more sensitive than manual assessment of data quality. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5214/ba5214bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5214/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5214/ba5214.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 57-66 [ doi:10.1107/S1399004714013923<http://dx.doi.org/10.1107/S1399004714013923> ] Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints H. S. Kim<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Kim%2C%20H%2ES%2E> and F. Gabel<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gabel%2C%20F%2E> Synopsis: The potentialities and limitations of biomacromolecular modelling of small-angle scattering data are reviewed and discussed with a focus on the impact of complementary NMR restraints and a hydration shell. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5229/ba5229bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5229/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5229/ba5229.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 67-75 [ doi:10.1107/S1399004714026959<http://dx.doi.org/10.1107/S1399004714026959> ] BioSAXS Sample Changer: a robotic sample changer for rapid and reliable high-throughput X-ray solution scattering experiments A. Round<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Round%2C%20A%2E>, F. Felisaz<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Felisaz%2C%20F%2E>, L. Fodinger<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Fodinger%2C%20L%2E>, A. Gobbo<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gobbo%2C%20A%2E>, J. Huet<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Huet%2C%20J%2E>, C. Villard<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Villard%2C%20C%2E>, C. E. Blanchet<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Blanchet%2C%20C%2EE%2E>, P. Pernot<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pernot%2C%20P%2E>, S. McSweeney<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=McSweeney%2C%20S%2E>, M. Roessle<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Roessle%2C%20M%2E>, D. I. Svergun<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Svergun%2C%20D%2EI%2E> and F. Cipriani<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Cipriani%2C%20F%2E> Synopsis: A robotic sample changer for solution X-ray scattering experiments optimized for speed and to use the minimum amount of material has been developed. This system is now in routine use at three high-brilliance European synchrotron sites, each capable of several hundred measurements per day. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5219/ba5219bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5219/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5219/ba5219.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/ba5219/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 76-85 [ doi:10.1107/S1399004714019609<http://dx.doi.org/10.1107/S1399004714019609> ] ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments A. De Maria Antolinos<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=De%20Maria%20Antolinos%2C%20A%2E>, P. Pernot<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pernot%2C%20P%2E>, M. E. Brennich<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Brennich%2C%20M%2EE%2E>, J. Kieffer<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Kieffer%2C%20J%2E>, M. W. Bowler<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Bowler%2C%20M%2EW%2E>, S. Delageniere<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Delageniere%2C%20S%2E>, S. Ohlsson<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Ohlsson%2C%20S%2E>, S. Malbet Monaco<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Malbet%20Monaco%2C%20S%2E>, A. Ashton<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Ashton%2C%20A%2E>, D. Franke<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Franke%2C%20D%2E>, D. Svergun<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Svergun%2C%20D%2E>, S. McSweeney<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=McSweeney%2C%20S%2E>, E. Gordon<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gordon%2C%20E%2E> and A. Round<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Round%2C%20A%2E> Synopsis: The ISPyB information-management system for crystallography has been adapted to include data from small-angle X-ray scattering of macromolecules in solution experiments. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5222/ba5222bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5222/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5222/ba5222.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 86-93 [ doi:10.1107/S1399004714016678<http://dx.doi.org/10.1107/S1399004714016678> ] Memprot: a program to model the detergent corona around a membrane protein based on SEC-SAXS data J. Pérez<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=P%26eacute%3Brez%2C%20J%2E> and A. Koutsioubas<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Koutsioubas%2C%20A%2E> Synopsis: Systematic SAXS simulations have been analysed over a wide range of parameters in order to better understand the detergent corona around a membrane protein. Online 1 January 2015 ________________________________ new mounts ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/gm5034/gm5034bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/gm5034/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/gm5034/gm5034.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/gm5034/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 94-103 [ doi:10.1107/S1399004714013728<http://dx.doi.org/10.1107/S1399004714013728> ] Acoustic transfer of protein crystals from agarose pedestals to micromeshes for high-throughput screening C. M. Cuttitta<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Cuttitta%2C%20C%2EM%2E>, D. L. Ericson<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Ericson%2C%20D%2EL%2E>, A. Scalia<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Scalia%2C%20A%2E>, C. G. Roessler<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Roessler%2C%20C%2EG%2E>, E. Teplitsky<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Teplitsky%2C%20E%2E>, K. Joshi<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Joshi%2C%20K%2E>, O. Campos<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Campos%2C%20O%2E>, R. Agarwal<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Agarwal%2C%20R%2E>, M. Allaire<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Allaire%2C%20M%2E>, A. M. Orville<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Orville%2C%20A%2EM%2E>, R. M. Sweet<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Sweet%2C%20R%2EM%2E> and A. S. Soares<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Soares%2C%20A%2ES%2E> Synopsis: An acoustic high-throughput screening method is described for harvesting protein crystals and combining the protein crystals with chemicals such as a fragment library. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5218/ba5218bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5218/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5218/ba5218.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 104-122 [ doi:10.1107/S1399004714010360<http://dx.doi.org/10.1107/S1399004714010360> ] Experimental phasing for structure determination using membrane-protein crystals grown by the lipid cubic phase method D. Li<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Li%2C%20D%2E>, V. E. Pye<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pye%2C%20V%2EE%2E> and M. Caffrey<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Caffrey%2C%20M%2E> Synopsis: Very little information is available in the literature concerning the experimental heavy-atom phasing of membrane-protein structures where the crystals have been grown using the lipid cubic phase (in meso) method. In this paper, pre-labelling, co-crystallization, soaking, site-specific mercury binding to genetically engineered single-cysteine mutants and selenomethionine labelling as applied to an integral membrane kinase crystallized in meso are described. An assay to assess cysteine accessibility for mercury labelling of membrane proteins is introduced. Online 1 January 2015 ________________________________ EM ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/gm5035/gm5035bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/gm5035/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/gm5035/gm5035.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 123-126 [ doi:10.1107/S1399004714018070<http://dx.doi.org/10.1107/S1399004714018070> ] Collaborative Computational Project for Electron cryo-Microscopy C. Wood<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Wood%2C%20C%2E>, T. Burnley<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Burnley%2C%20T%2E>, A. Patwardhan<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Patwardhan%2C%20A%2E>, S. Scheres<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Scheres%2C%20S%2E>, M. Topf<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Topf%2C%20M%2E>, A. Roseman<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Roseman%2C%20A%2E> and M. Winn<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Winn%2C%20M%2E> Synopsis: The Collaborative Computational Project for Electron cryo-Microscopy (CCP-EM) is a new initiative for the structural biology community, following the success of CCP4 for macromolecular crystallography. Progress in supporting the users and developers of cryoEM software is reported. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5227/ba5227bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5227/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5227/ba5227.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 127-135 [ doi:10.1107/S1399004714025280<http://dx.doi.org/10.1107/S1399004714025280> ] A national facility for biological cryo-electron microscopy H. R. Saibil<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Saibil%2C%20H%2ER%2E>, K. Grünewald<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gr%26uuml%3Bnewald%2C%20K%2E> and D. I. Stuart<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Stuart%2C%20D%2EI%2E> Synopsis: This review provides a brief update on the use of cryo-electron microscopy for integrated structural biology, along with an overview of the plans for the UK national facility for electron microscopy being built at the Diamond synchrotron. Online 11 December 2014 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5226/ba5226bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5226/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5226/ba5226.pdf> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 136-153 [ doi:10.1107/S1399004714021683<http://dx.doi.org/10.1107/S1399004714021683> ] Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions A. Brown<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Brown%2C%20A%2E>, F. Long<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Long%2C%20F%2E>, R. A. Nicholls<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Nicholls%2C%20R%2EA%2E>, J. Toots<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Toots%2C%20J%2E>, P. Emsley<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Emsley%2C%20P%2E> and G. Murshudov<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Murshudov%2C%20G%2E> Synopsis: A description is given of new tools to facilitate model building and refinement into electron cryo-microscopy reconstructions. Online 1 January 2015 ________________________________ dynamics ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5228/ba5228bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5228/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5228/ba5228.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/ba5228/stdsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 154-161 [ doi:10.1107/S1399004714026662<http://dx.doi.org/10.1107/S1399004714026662> ] Structure calculation, refinement and validation using CcpNmr Analysis S. P. Skinner<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Skinner%2C%20S%2EP%2E>, B. T. Goult<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Goult%2C%20B%2ET%2E>, R. H. Fogh<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Fogh%2C%20R%2EH%2E>, W. Boucher<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Boucher%2C%20W%2E>, T. J. Stevens<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Stevens%2C%20T%2EJ%2E>, E. D. Laue<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Laue%2C%20E%2ED%2E> and G. W. Vuister<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Vuister%2C%20G%2EW%2E> Synopsis: This report describes the working of the program CcpNmr Analysis for both NMR chemical shift assignment and structure determination of biological macromolecules. Online 1 January 2015 ________________________________ [thumbnail of article figure]<http://journals.iucr.org/d/issues/2015/01/00/ba5225/ba5225bdy.html> [[HTML version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5225/index.html>[[PDF version]]<http://journals.iucr.org/d/issues/2015/01/00/ba5225/ba5225.pdf>[[Supplementary Material]]<http://journals.iucr.org/d/issues/2015/01/00/ba5225/stdsup.html>[[Video data files]]<http://journals.iucr.org/d/issues/2015/01/00/ba5225/vidsup.html> [[Open access]] <http://journals.iucr.org/services/openaccess.html> Acta Cryst. (2015). D71, 162-172 [ doi:10.1107/S1399004714026777<http://dx.doi.org/10.1107/S1399004714026777> ] In pursuit of an accurate spatial and temporal model of biomolecules at the atomistic level: a perspective on computer simulation A. Gray<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Gray%2C%20A%2E>, O. G. Harlen<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Harlen%2C%20O%2EG%2E>, S. A. Harris<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Harris%2C%20S%2EA%2E>, S. Khalid<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Khalid%2C%20S%2E>, Y. M. Leung<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Leung%2C%20Y%2EM%2E>, R. Lonsdale<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Lonsdale%2C%20R%2E>, A. J. Mulholland<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Mulholland%2C%20A%2EJ%2E>, A. R. Pearson<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Pearson%2C%20A%2ER%2E>, D. J. Read<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Read%2C%20D%2EJ%2E> and R. A. Richardson<http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Richardson%2C%20R%2EA%2E> Synopsis: The current computational techniques available for biomolecular simulation are described, and the successes and limitations of each with reference to the experimental biophysical methods that they complement are presented. Online 1 January 2015
