This EMBO Workshop will cover the use of small angle scattering (SAS) of both neutrons and X-rays for the determination of the structures of biological macromolecules. Particular attention will be paid on this course to sample preparation and the analysis and interpretation of SAS data in a biological context. The aim of this course is to enable the participants to maximise the information gained from the SAS technique in their future experiments.

Small angle scattering is a powerful technique for determining the structures of biological molecules in solution. Not only can small angle scattering provide precise information concerning the size, molecular weight, volume and shape of single molecules but it can also provide detailed information from large, multi-component macromolecular complexes. For these purposes the scattering properties of neutrons are particularly well suited. Through the use of specific isotope labeling techniques and solvent contrast variation it is possible to determine the structural organisation of specific components within a large macromolecular assembly.

Taking advantage of the location of the European Synchrotron Radiation Facility (ESRF) and the Institut Laue Langevin (ILL) on the same scientific campus in Grenoble, this course will focus on the complimentary use of X-ray and neutron small angle scattering for the determination of the structures of biological macromolecules. Through the use of lectures, tutorials and practicals it is intended to teach scientists new to the technique how to optimize their experiments to gain the maximum amount of information from these techniques. In particular the course will focus on:

• Small angle scattering theory
• Sample requirements for a successful small angle scattering experiment
• Data analysis, model building and interpretation
• Isotope labelling strategies for small angle neutron scattering
• Analysing small angle scattering in conjunction with data obtained from other techniques (NMR, AUC, EM, SEC-MALLS)

Register by: 1 March 2015

The workshop aims at enabling structural biologists to fully exploit the latest instrumentation and software development at the SNS and HFIR facilities at Oak Ridge National Laboratory. Attendees will participate in lectures and tutorials focusing exclusively on neutron techniques applied in structural biology. The workshop is designed for graduate students, post-doctoral fellows and faculty new to or with limited experience of neutron scattering.

General Information

The unique potential of neutron scattering in structural biology arises from the strong interaction of neutrons with hydrogen (H) and its deuterium (D) isotope. This property makes the information available from neutron scattering unique and a valuable complement to data obtained from other structural techniques. Individual hydrogen/deuterium atoms are visualized in neutron density maps from crystallographic data at the resolution typical of most protein structures (2.0 -2.5 Ã...).Using H/D exchange  and contrast variation, proteins and nucleic acids are sequentially modeled and mapped in large biological complexes using small angle neutron scattering, protein-membrane interactions are revealed using Reflectometry and protein and water dynamics measured using spectroscopy.

The workshop includes a symposium, lectures and tutorials and tours of the High Flux Isotope reactor and Spallation Neutron Source, the world’s leading neutron research facilities.

The workshop is designed for graduate students, post-doctoral researchers and faculty with knowledge of protein function and structure but no or limited experience of neutron sciences.

Subjects include:

• Crystallography
• Small Angle Scattering
• Reflectometry
• Spectroscopy
• Imaging
• Labeling techniques

Course Objectives

1. Educate participants in neutron scattering techniques, instrumentation and data collection, analysis and interpretation.
2. Expose participants to cutting-edge research in neutron structural biology.
3. Build interactions between participants, their university groups, and ORNL neutron scattering experts to develop new research projects.

Application deadline: April 10, 2015

Travel and accommodation expenses are supported for selected participants from the United States. International applications are welcome. However the course organization is not able to support travel or accommodation.

The number of participants will be limited to 15. There is no registration fee for all selected participants.

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The application package consisting of 1) Information form, 2) CV, 3) Applicant motivation letter (1/2 to 1 page), 4) Principal Investigator letter of support (for graduate students only; 1/2 to 1 page), should be sent electronically to meilleurf@ornl.gov before April 10, 2015.

8th annual CCP4 USA Crystallography School

The first two days will be dedicated to data collection and processing. The rest of the school will focus on structure solution, refinement and validation.

The course is intended mainly for graduate students, postdoctoral researchers and young scientists in the area of structural biology from all across the globe. The school is not meant as an introductory level course to protein crystallography. It is designed more for applicants with reasonable expertise in crystallography and experience with the CCP4 suite. The purpose of the school is to address specific problems that the applicants face while collecting diffraction data and while solving and refining novel structures. Applicants with crystals for data collection or with already collected data will be given strong consideration, although these are not mandatory requirements.

Several of the leading PX software developers from around the world will present lectures and tutorials on their software and will also be available to help with problems during hands-on sessions of the school.

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Converging Disciplines for the Advancement of Inter-RNA Interactions

Connecting G Protein-Coupled Receptor Mechanisms to Physiological Functions

New Frontiers in GPCR Signaling: From Biased Agonism to Disease Progression

Workshops on Membrane Protein Technologies: April 9, 2015

MPS 2015 Meeting: April 10-12, 2015

The goal of the meeting is to share developments in technologies appropriate for the determination of the structure of membrane proteins, membrane protein complexes with other proteins and ligands, and to highlight recent results. The meeting brings together keynote lectures, oral presentations and poster presentations. Subjects range from membrane protein construct design, expression to mass spectrometry, spectroscopic, X-ray diffraction, electron microscopy imaging, and hybrid approaches.Â

Industry sponsors are invited to participate fully in the meeting. Students and postdoctoral scholars are encouraged to submit abstracts for oral or poster presentations. Workshops are offered that share experience and training in most recent developments in areas including but are not limited to membrane protein expression systems, protein purification, solubilization, crystallization, LCP, free electron laser sample preparation, and NMR.

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The aim of the School is to bring together experts and young scientists interested in exploiting the anomalous signal from light atoms (e.g. S, P, Ca, K, Mg) native to the protein or crystal for macromolecular structure determination using soft (wavelengths > 1.5Ã...) X-rays in order to help train the next generation of scientists in this maturing field. The 5th Winter School on Soft X-rays in Macromolecular Crystallography is a continuation of similar workshops held in Europe since 2003 as indicated:

1st Winter School:Â Bressanone/Brixen, Italy; Feb. 25-27, 2003

2nd Winter School: Seefeld, Austria; March 22-25, 2006

3rd Winter School:Â Berlin, Germany; February 18-20, 2009

4th Winter School:Â Grenoble, France, February 6-8, 2012

Topics Covered

Source/Beamline Considerations These lectures and Case Studies will cover the optimization of the experiment setup in terms of the hardware, choice of wavelength and other source specific parameters.

Data Collection Strategies This lecture will cover techniques and problems associated with collecting sulfur-SAD data including crystal centering, data collection setup and methods used to increase the anomalous scattering signal to noise ratio in the data. The lecture will highlight common areas where problems can occur and suggest how best to eliminate them.

Data Reduction Theory and Strategies These lectures and Case Studies will focus on the data reduction process (indexing, integration and scaling) using several popular data reduction programs as examples, highlighting critical program input parameters and program output. The lecture will highlight common areas where problems can occur and suggest how best to eliminate them. New methods such as Multi-Crystal and Single Crystal Multi-dataset averaging will be described.

Anomalous Substructure Determination & Phasing This lecture and Case Study will describe the use of SHELXCDE [9] and HKL2MAP to determine the anomalous scattering substructure, the correct handedness of the anomalous scattering substructure, the generation of initial protein phases and interpreting the quality of the resulting electron density map.

Smart Chemistry, Better Life

IUPAC 48th General Assembly 6-13 August 2015 and 45th World Chemistry Congress 9-14 August 2015

Conference Topics

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• Physical Chemistry
• Molecular Synthesis
• Advances in Inorganic Chemistry
• Materials for Energy and Environment
• Analytical Chemistry & Environment
• Macromolecular Science and Technology
• Chemistry of Life
• Nanoscience and Materials
• Open Innovation for Enlightening Chemistry Education
• Green Chemistry for World Needs
• Chemistry for Industry Innovation
• Women in Chemistry: Gaining Momentum

The course will be organised by Lari Lehtiö, Kristian Koski, Tiila Kiema, Ari-Pekka Kvist and Rik WierengaÂ

The course is supported by Biostruct-X, Biocenter Oulu, and the University of Oulu

There will be an international X-ray course at the Faculty of Biochemistry and Molecular Medicine of the University of Oulu, Oulu, Finland. The course will focus on data collection and data processing using iMOSFLM and XDS, to be complemented by lectures and tutorials on experimental phasing (SHELX) and molecular replacement phasing (CCP4). In addition there will be lectures on new techniques (XFEL diffraction and neutron crystallography). On the last day of the course there will be a remote data collection demonstration at Diamond Light Source, Oxford. The outline of the course follows the previous format, aiming for approximately 16-20 students, who will be provided with a computer in our linux class room. Data collection from own crystals will be possible using our in-house Bruker microfocus X-ray generator or remotely at Diamond.

Current approximate outline:

Monday, May 18:
Basic concepts of biomolecular crystallography, by Bernhard Rupp (USA)
Emerging techniques: XFEL by Janos Hajdu (Uppsala, Sweden): “The basic principles of the XFEL technology and molecular imaging"

Tuesday, May 19/Wednesday, May 20 (data processing):
XDS, Manfred Weiss, BESSY, Berlin, Germany (also XDSapp as available at Bessy)
iMOSFLM, Harry Powell (LMB, Cambridge, UK) Â (also data processing pipelines at Diamond)
Tuesday afternoon lecture by Bernhard Rupp on ligand binding studies

Wednesday, May 20/Thursday, May 21: (experimental and molecular replacement phasing)
Experimental phasing by SHELX, Thomas Schneider (EMBL, Hamburg)
Molecular replacement phasing by CCP4, Andrey Lebedev (CCP4, STFC)
Wednesday afternoon lecture on neutron crystallography by Dr. Zoe Fisher (ESS, Lund)
Thursday afternoon lecture by Thomas Schneider on the X-ray beamlines at EMBL, Hamburg
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Friday, May 22:
Remote data collection at Diamond (Martin Walsh, Diamond)
Crystal sample management and data tracking from crystal to PDB by xtalPiMS (Ed Daniel, Oulu)
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Throughout the course students will have time to work on their own topics in the linux class room and we will also provide the opportunity to collect data with our own equipment. Crystals that should be used for data collection in house or at Diamond should be available for freezing on the first day of the course or should be sent in advance to Oulu.

There will be a registration fee of 350Euro to cover the costs of accommodation and meals. We will try to make available fellowships to cover these costs. When applying to attend this course follow the instructions attached below.  Please provide information on crystals and/or datasets that you would like to send in advance. Indicate also if such a fellowship is needed when being accepted for this course. In case of oversubscription, students with own crystals and / or own data sets will be prioritised.

Please apply by by 10.01.2015

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The workshop will consist of both plenary and parallel sessions. The plenary session will begin with presentations on science topics in research fields that the beamlines are designed to address, followed by facility presentations to update the community about the early scientific capabilities at the suite of ABBIX beamlines and, in addition, of the Life Science and Biomedical Technology Research Resource (LSBR), sponsored by the NIH and the Department of Energy Office of Biological and Environmental Research (DOE BER). Two parallel sessions on Wednesday afternoon will focus on MX and X-ray scattering, consisting mainly of presentations that will address specific opportunities in these areas. These will be followed by two more parallel sessions on Thursday morning, also focusing on MX and X-ray scattering, consisting mainly of contributions. If you wish to give a contributed presentation during one of the parallel sessions, please submit an abstract.

The parallel sessions are designed to provide forums to facilitate more detailed discussions about potential first experiments at specific beamlines and the formation of the experiment teams. Specifically, each parallel session group will be charged to:  ​​​​​​​​​​

• ​​​Identify key research projects and the associated first experiments that may be performed at the suite of ABBIX beamlines, emphasizing those projects that will take advantage of NSLS-II properties and ABBIX beamline capabilities.
• Facilitate the formation of research teams to generate first experiment proposals for submission.
• Identify key additional team members in such areas as theory and analysis, ancillary measurements, and specimen preparation, needed to achieve the research goals.

Confirmed invited speakers:Â Karen Allen (Boston Univ), Martin Caffrey (Trinity College Dublin), Wayne Hendrickson (Columbia Univ), Andre Hoelz (California Inst Tech), Shenping Liu (Pfizer), Lee Makowski (Northeastern Univ), Anna-Marie Pyle (Yale Univ), Christian Riekel (ESRF), Thomas Schneider (EMBL-Hamburg), John Tainer (Scripps Research Inst), Da-Neng Wang (New York Univ), Michael Wiener (Univ Virginia).

The expected outcome from this workshop is two-fold: (a) a concise workshop report outlining how ABBIX beamlines will help to address outstanding problems in life sciences, and (b) a list of potential first experiments along with the corresponding research teams.

Organizers:

Lonny Berman
ABBIX Project Manager
Photon Sciences Directorate
Brookhaven National LaboratoryÂ

Sean McSweeney
Associate Photon Division Director for Structural Biology Program
Photon Sciences Directorate
Brookhaven National Laboratory

Deep Sequencing Meets Structural Biology

• Deep sequencing for modeling and refinement of macromolecular structures
• Membrane protein structure and function using complementary methods
• Technological advances in XFEL, Cryo-EM, NMR, SAXS, MS, MX and macromolecular complexes
• Combining low and high resolution data and modeling for structural biology
• Synergistic use of 3D structures and deep sequencing to realize personalized medicine
• Protein design and deep sequencing
• Cancer, antibiotic resistance and drug discovery

• Cryo-EM developments for structural biology [Sponsored by FEI]
• PHENIX: Automated determination of molecular structures
• HKL3000: From X-ray diffraction images to structure determination in minutes
• Approaches to the translation of deep sequencing data into three-dimensions
• Protein expression and characterization workshop
• Proteopedia: A Scientific Wiki Bridging the Rift Between 3D Structure & Function

BioStruct-X (www.biostruct-x.eu) is an integrated project funded by the Seventh Framework Programme of the European Commission for transnational access to biological synchrotron X-ray radiation facilities. The BioStruct-X consortium coordinated by EMBL-Hamburg has 19 partners from 11 EU member and associated states providing integrated access via 42 installations in four key areas: macromolecular X-ray crystallography, small angle X-ray scattering, X-ray imaging, protein production and high-throughput crystallisation. In addition to the transnational access, BioStruct-X partners are involved in joint research activities aimed at novel developments in synchrotron instrumentation, automation of the experiment and high-throughput software services.

The X-ray based structural biology activities supported in BioStruct-X are core technologies used in many pharmaceutical and biotech companies. The workshop will promote the exchange of knowledge and approaches, either available or being established, between BioStruct-X consortium and industrial partners.

The Workshop will take place at the premises of the DESY synchrotron facility in Hamburg operating the presently world brightest storage ring PETRA III. A tour to the biological beamlines running at PETRA III will be included in the program. There will be a poster session and ample advertizing possibilities for the companies.

Further information about the workshop, including its program, organizers, registration and abstract submission are available at:

http://www.biostruct-x.eu/industry_workshop2015

We look forward to welcoming you to the workshop!

Join VIB at its first conference on ‘Structural dynamics in cellular communication’ that will take place in an architecturally significant venue in the heart of Europe (Brussels, Belgium) from 9-10 February, 2015.

The conference will cover the latest advances in protein science, focusing on systems structural biology, the functional role of structural dynamics, the organization of complexes and key technological advances. During four plenary sessions this first edition will handle the following topics: Â macromolecular machines and assemblages; protein network dynamics; protein fluctuations and function; and membrane proteins and complexes.

Ada Yonath, Weizmann Institute of Science, Israel

Lewis Kay, University of Toronto, Canada

Sheena Radford, University of Leeds, UK

Brian T. Chait, Rockefeller University, USA

Susan Buchanan, National Institutes of Health, USA

Thomas Marlovits, Center for Structural Systems Biology, Hamburg, Germany

*The 2014 BCA-BSG Winter Meeting will take place on the European Photon and Neutron (EPN) Campus (hosting the European Synchrotron Radiation Facility and the Institute Laue Langevin), Grenoble, France on 15-17 December 2014. The meeting will be themed around opportunities for Structural Biology at large-scale research infrastructure and will include sessions addressing the combination of structural information from X-rays & neutrons in Structural Biology, Structural Biology on the EPN Campus, and Emerging Techniques in Structural Biology.

Confirmed speakers include:

• Arwen Pearson, CUI, Hamburg, Germany
• Cecilia Casadei, University of Leicester, UK
• Julia Richardson, University of Edinburgh, UK
• Selma Maric, Karolinska Institute, Sweden
• Stephen Cusack, EMBL, Grenoble
• Andrea Dessen, IBS, Grenoble
• Catarina da Silva, CEA, Grenoble
• Antoine Royant, IBS, Grenoble
• Gemma Newby, ESRF, Grenoble
• Manfred Burghammer, ESRF, Grenoble
• Matthew Bowler, EMBL, Grenoble
• Ulrich Zander, ESRF, Grenoble
• Estelle Mossou, University of Keele, UK/ILL, Grenoble
• Helmut Schober, Director of Science, ILL, Grenoble
• Elizabeth Duke, Diamond Light Source, UK

The first half of the meeting - supported by the UK Science & Technology Funding Council (STFC) - aims at presenting the strategic significance to the structural biology community of UK investment in large-scale research infrastructure. This part of the meeting will include visits to ESRF and ILL Experimental Facilities, a round table discussion and speakers including:

• Florent Bernaudat, Partnership for Structural Biology, Grenoble
• Harald Reichert, ESRF, Grenoble
• Colin Miles, BBSRC, UK
• Pamela Williams, Astex, UK
• David Scott, University of Nottingham, UK
• Adrian Mancuso, European XFEL, Hamburg, Germany
• Andrew Harrison, Diamond Light Source, UK
• Gordon Leonard, ESRF, Grenoble
• Trevor Forsyth, ILL, Grenoble

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The deadline for registration is the 8 December.

The programme includes a poster session. Contributions from younger and more senior scientists on any aspect of Structural Biology are actively encouraged.

 In order to help reduce the costs of attending the meeting, the registration fee (32EUR for students; 64EUR for regular participants) will include the cost of all meals during the meeting, including the meeting dinner on 16 December and as many participants as possible will be housed - at participants' own cost - in the cost effective ESRF/ILL Guesthouse. The registration fee also includes membership of the BCA for the year 2015.

Five Travel Bursaries, each of up to £200, are available from the BCA to support participation in the meeting by research students and postdoctoral workers who are BCA members. Please see http://crystallography.org.uk/prizes/bursaries/abbf-bursaries/ for details.

This International School will focus on the fundamentals of crystallization from solution and its applications to the field of the crystallization of biological macromolecules.

ISBC2015 will provide five days of lectures and practical demonstrations related to the crystallization of biological macromolecules, biominerals and biomimetic materials, with one full day devoted to case studies on the crystallization of membrane proteins, viruses and large macromolecular complexes

We invite students from all over the world to join us to learn from selected international experts, to hear case study presentations, to watch practical hand-on demonstrations, to participate in round-table discussions and to present their research results in the dedicated poster sessions.

The language of the School will be English.

The School will be held from the 24th to the 29th of May 2015 at Hotel San Antón in Granada (Spain).

Topics of the School

ISBC Granada 2015 will focus on the fundamentals of crystallization from solution and its applications for the crystallization of biological materials.

• Nucleation: Classical and non-classical approaches
• Crystal growth kinetics and mechanisms
• Properties of macromolecular solutions relevant to crystallization
• Screening: Searching for crystallization conditions
• Crystallization techniques: Batch, Vapour and Counter Diffusion, How do they work?
• Crystallization and diffusion transport: gels, microfluidics and microgravity
• Crystallization of large crystals for Neutron diffraction and tiny crystals for XFEL
• Polymorphism in protein crystals
• Robotics and crystallization
• Membrane Protein Crystallization: case studies
  
• Lipid cubic phase, bicelles and detergents
• Crystallization of Large Macromolecular Complexes:
• In vitro and in vivo studies of Biomineralisation processes