Free educational webinar to be presented by Dr Wei Liu titled “Femtosecond crystallography of membrane proteins in lipidic cubic phase (LCP).”

Despite recent technological advances in heterologous expression, stabilization and crystallization of membrane proteins (MPs), their structural studies remain difficult and require new transformative approaches. During the past two years, crystallization in lipidic cubic phase (LCP) has started gaining widespread acceptance, owing to the spectacular success in high-resolution structure determination of G protein-coupled receptors (GPCRs) and to the introduction of commercial instrumentation, tools and protocols. The recent appearance of X-ray free-electron lasers (XFELs) has further enabled structure determination from substantially smaller crystals than previously possible, offering exciting new opportunities in structural biology. The unique properties of LCP material have been exploited to develop special protocols and devices that have established a new method of serial femtosecond crystallography of MPs in LCP (LCP-SFX). In this method, microcrystals are generated in LCP and streamed continuously inside the same media across the intersection with a pulsed XFEL beam at a flow rate that can be adjusted to minimize sample consumption. Pioneering studies that yielded the first room temperature GPCR structures, using a few hundred micrograms of purified protein, validate the LCP-SFX approach and make it attractive for structure determination of difficult-to-crystallize MPs and their complexes with interacting partners. Together with the potential of femtosecond data acquisition to interrogate unstable intermediate functional states of MPs, LCP-SFX holds promise to advance our understanding of this biomedically important class of proteins.

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The European Learning Laboratory for the Life Sciences (ELLS), in collaboration with La Casemate Grenoble, invites European secondary school science teachers to apply for the ELLS LearningLAB “Structural biology â€" shining light onto the fabric of life” at EMBL Grenoble (France).

The course will provide an interactive introduction to the field of structural biology. The professional training course for secondary school science teachers will consist of a mix of seminars by EMBL scientists, hands-on activities and visits to world-class research facilities on the European Photon & Neutron Science Campus. The programme will cover a wide range of topics and highlight the use of high-energy X-ray sources and protein crystallography to study virus structures on the atomic scale.

During the 2-day course, a combination of seminars, discussions and hands-on activities will:

• Introduce you to X-ray crystallography and its great potential to gain insights into the structure and function of viral proteins and antiviral drug design;
• Update your knowledge on current biological research and get you in touch with research scientists;
• Illustrate a range of classroom activities and experiments and equip you to use the presented resources to support your teaching of biology;
• Include visits to world-class research facilities at the European Molecular Biology Laboratory Grenoble and the European Synchrotron Radiation Facility (ESRF);
• Give you the opportunity to develop your own scientific quiz and make it available to your students using the EMBL LearnApp;
• Allow you to network and share your experiences with teachers colleagues.Location: EMBL Grenoble (European Photon & Neutron Science Campus) / La Casemate Grenoble

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Course language: English  (teaching resources will be provided in English and French)

Course fee: free attendanceÂ

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Keynote speakers: Raymond C. Stevens and John C. H. Spence

The aim is to provide MX users with sufficient training to be able to operate any of the Diamond MX beamlines efficiently and to get the most benefit from their beamtime. The training will involve hands-on sessions on the suite of five operational MX beamlines (http://www.diamond.ac.uk/mx-home/) as well as offline software sessions.

Sessions include:

4th December, day session on MX beamlines:

 *  MX software: automation in data analysis
 *  Mini-Kappa goniometry / Anomalous data collection
 *  Sample humidity control (HC1)
 *  I24 new end station
 *  In-situ diffraction
 *  Experiment database: new ISPyB

5th December, morning session: Hands on software in
three tutorial sessions:

 *  CCP4: MR and experimental phasing (CCP4 team)
 *  Manual processing iMosflm (Harry Powell)
 *  Multi crystal analysis / BLEND (James Foadi)


Registration is free-of-charge with lunch provided on the 4th and 5th December, and accommodation and dinner for the nights of the 3rd and 4th December. Travelling expenses within the UK will also be provided. The training is targeted at all users, and is not limited to students and post docs. It is essential that each BAG sends at least one representative per calendar year.

Registration
Places are limited to twenty five participants. The registration deadline is on the 20th November.
Registration is now open

Chair:Â Alexandre Bonvin

Vice Chair:Â Valerie Daggett

The Gordon Research Conference on Computational Aspects of Biomolecular NMR provides a unique forum for the presentation and discussion of emerging methods at the intersection of experimental Nuclear Magnetic Resonance (NMR), computational methods and other complementary biophysical techniques.

NMR is one of the most versatile methods for the investigation of biomolecular systems, whether these are proteins, nucleic acids, glycans, membranes, or functioning cellular and in vivo systems. In the modern toolbox of researchers, NMR is one of the well-established methods, which, in combination with other complementary biophysical and computational methods, contributes to our understanding and diagnosis of disease, the development of therapeutics to combat disease and the engineering of novel or improved biomolecules with a wide range of applications in heath, food and materials. NMR can provide unique structural, dynamical and functional information to achieve these goals. Continuous advances are pushing back the frontiers of NMR in numerous application fields, enabling the study of systems of ever increasing complexity and/or in more natural, cellular environments. All these can, however, only be achieved by integrating new types of data and learning to use them in combination with other experimental information sources. Computational methods, whose importance for the field has been recognized by the awarding of the 2013 Nobel prize in chemistry, play here a key role in this integration process.

This GRC conference will bring together practitioners in NMR, computational structural biology and other complementary biophysical techniques for the purpose of generating new ideas and promoting collaborations in order to generate the next generation of integrative methods that will allow us to tackle ever more challenging systems.

The 2015 meeting, which will take place at the beautiful location of Il Ciocco in Toscane. It will have sessions devoted to advances in integrative structural biology, complementary biophysical techniques, frontiers in solid state NMR, signal processing, intrinsically disordered systems and interactions, ligand interactions and metabolomics, conformational variability and challenges in structure determination. Further, the importance of NMR for industry will be highlighted in a dedicated session. The prominent list of speakers, along with the small format of the conference, will provide unique opportunities for graduate students, postdocs, and those new to this research area, to discuss their research with leaders in the field. Extensive poster sessions, along with promoted talks, will facilitate this process.

A Gordon Research Seminar on "Molecular Simulation for the Interpretation of NMR Data" will precede the conference. Besides providing an excellent opportunity for graduate students and postdocs to become familiar with the atmosphere of a Gordon Conference, the Seminar will feature keynote talks from leaders in the field and speaking slots for a number of students and postdocs. Application for the Seminar and Conference are separate, and those interested should consult the Seminar description.

Preliminary Program

A list of preliminary session topics and speakers is displayed below (discussion leaders are noted in italics). The detailed program is currently being developed by the Conference Chair and will be available by February 7, 2015. Please check the conference website for updates.

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• Keynote Session: Advances in Integrative Structural Biology
  (Antonio Rosato / Andrej Sali / Adam Lange)
• Conformational Variability and Dynamics
  (Andrew Baldwin / Christian Griesinger / Claudio Luchinat / Arthur Palmer / David Fushman)
• NMR and Computations in Industry
  (Ben Davis / Greg Siegal / Michael Schaefer / Chun-Wa Chung)
• Ligand Interactions and Metabolomics
  (Giovanna Musco / Robert Konrat / James Prestergard / Rafael Bruschweiler / David Wishart)
• Signal Processing
  (Christina Redfield / Jeffrey Hoch / Tatyana Polenova / Vladislav Orekhov)
• Pushing the Limits of Solid State NMR
  (Tatyana Polenova / Marc Baldus / Mei Hong / Lyndon Emsley / Anne Ulrich)
• Frontiers of NMR: Complementary Methods
  (Alexandre Bonvin / Pau Bernardo / Alexander Leitner / Holger Stark)
• Challenges in Structure Determination
  (Torsten Herrmann / Ad Bax / Tobias Madl / Chad Rienstra / Angela Gronenborn)
• Intrinsically Disordered Systems and Interactions
  (Valerie Daggett / Frans Mulder / Carine Van Heijenoort / Martin Blackledge)

To coincide with the grand opening of Beamline 7.2W: macromolecule crystallography (BL7.2W: MX) and celebration of the International Year of Crystallography 2014, SLRI would like to announce the AWPX2014. The

This course is intended for young scientists and aims to provide better understanding of key concepts in protein crystallography with hands-on experience in X-ray data collection at BL7.2W: MX, data processing and structure determination.

Keynote Speaker: Prof. Dr. Chun-Jung Chen (NSRRC, Taiwan)

On the occasion of the 25th anniversary of the internationally known HERCULES Course, we will organize a three-week HERCULES School from July 6 to 24,2015 in Hsinchu, Taiwan where the National Synchrotron Radiation Research Center (NSRRC) is located. The NSRRC is a national laboratory which operates a 1.5-GeV synchrotron named Taiwan Light Source and is constructing another 3-GeV one called Taiwan Photon source. This 2015 Asia-Pacific Edition of HERCULES in TAIWAN, "Neutron and Synchrotron Radiation for Physics and Chemistry of Condensed Matter and Biomolecular Structure and Dynamics," is a three-week training course including a week of practicals and tutorials. It will be opened to PhD students, postdoctoral, young scientists working in the fields relate to physics, chemistry, biology, and materials science. The language of the course is English.

25 Years of Neutron & Synchrotron Radiation Science

This school provides training for students, postdoctoral and senior scientists from European and non-European universities and laboratories, in the field of Neutron and Synchrotron Radiation for condensed matter studies (Biology, Chemistry, Physics, Materials Science, Geosciences, Industrial applications).

The 1-month school includes lectures (60%), hands-on practicals and tutorials at partner institutes (ESRF, ILL in Grenoble, Soleil and LLB near Paris, SLS in Switzerland) and Grenoble Laboratories (CEA, CNRS, EMBL, IBS).

The school includes a common part and two parallel sessions:
Biomolecular, soft condensed matter structure & dynamics,
Physics and chemistry of condensed matter

HERCULES is a yearly event, established in 1991.

The Australian Synchrotron's annual User Meeting showcases some of the best research and investigations undertaken at the facility, and provides our user community with updates on the latest developments and technical advances in synchrotron science, both at home and at our sister light sources overseas. Organised by the Australian Synchrotron User Advisory Committee, the 2014 meeting will again be held at the award-winning National Centre for Synchrotron Science (NCSS).

Topics:

• Advanced Materials
• Beamlines, Instrumentation and Techniques
• Biological Systems
• Earth and Environment
• Energy Materials
• Imaging
• Radiotherapy and Radiobiology
• Soft Matter
• Structural Biology
• Surface Science

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Complementary seminar presented by TA Instruments

This seminar includes a range of topics and will cover techniques available for the characterisation of Biomolecular interactions - with a focus on the use of Calorimetric tools such as ITC and DSC.

Attendance is free, but as numbers will be limited registration will be offered on a first come first serve basis.

LUNCH will be provided and the meeting will conclude with a free tour of the Williams F1 collection.
Agenda
________________________________
Studying Biomolecular Interactions by ITC
- John Ladbury, MD Anderson Cancer Centre, University of Texas
Protein-protein interactions in membrane trafficking
- David Owen, Cambridge Institute for Medical Research, Cambridge University
ITC for Enzyme Kinetics
- Malin Suurkuusk, TA Instruments
DSC Characterization of the Structure/Function Relationship for Proteins
- Dile Holton, TA Instruments
Studying interactions between protein, small molecules and water by DSC
- Robert Falconer, Chemical & Biological Engineering, Sheffield University
ITC and DSC data analysis -Tips and Tricks on Model Selection
- Malin Suurkuusk, TA Instruments
Free Tour of Williams F1 Museum

This year, the topic for the Study Weekend is "Advances in Experimental Phasing". In keeping with previous CCP4 meetings, the lectures will focus on the presentation and discussion of advanced methods and techniques developed and used by the leaders in the field.

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Scientific Organisers

Dr Thomas Schneider (EMBL Hamburg, Germany)
Dr Airlie McCoy (University of Cambridge, UK)

The biennial "EFMC International Symposium on Medicinal Chemistry" (EFMC-ISMC) is a key Symposium in its field and attracts traditionally between 1200 and 1400 participants, from industry and academia. Recent EFMC-ISMC meetings have been organised in different countries including Denmark (Copenhagen/Malmö, 2004), Turkey (Istanbul, 2006), Austria (Vienna, 2008), Belgium (Brussels, 2010) and the most recent one in Germany (Berlin, 2012).

The 2014 edition will continue the tradition established by these biennial symposia and will cover drug discovery advances in the major therapeutic areas, including neglected diseases, CNS disorders, inflammation, metabolic disorders, and oncology. EFMC-ISMC 2014 will present the most recent advances in lead identification and optimization strategies, drug design and profiling technologies, and illustrate the impact of biomarkers and imaging at the interfaces between chemistry, biology and experimental medicine. Particular emphasis will be put on first time disclosures, recent highlights in medicinal chemistry, and organic synthesis which had a strong impact on medicinal chemistry.

This symposium is recognised worldwide as one of the leading Medicinal Chemistry meetings, as proven by its large international attendance.

We are very pleased to announce the first joint CCP4 & Diamond Light Source workshop on practical macromolecular crystallography, to take place at Diamond this December.

The workshop will consist of presentations and tutorials delivered by experts in the field, plus two days of data collection time at Diamond's excellent MX beamlines. Students will be able to work alongside experts on their own projects, tackling all aspects of structure solution, from data collection through to phasing, refinement and validation.

The course is intended mainly for graduate students, postdoctoral researchers and early career scientists in the area of structural biology. Some experience of crystallography and the use of CCP4 software is expected, and applications from students who can bring an interesting project with them (crystals and possibly previously collected datasets) will be favoured. Students will have access to Diamond's computing facilities for the duration of the course, with access to most major MX software packages.

Plenary Speakers

We are glad to announce that the following experts have already confirmed to give a lecture during the 10^th European Biophysics Congress.

Marileen Dogterom, FOM Institute AMOLF, Amsterdam, the Netherlands
Christian Eggeling, University of Oxford, UK
Martin Fussenegger, Swiss Federal Institute of Technology (ETH) Zurich, Switzerland
Raymond Goldstein, University of Cambridge, UK
Angela M. Gronenborn, University of Pittsburgh, USA
Gunnar von Heijne, Stockholm University, SE
Matthias Rief, Technical University Munich, Germany

Introduction

Recently crystallography and spectroscopy have reached a level of experimental sophistication and theoretical and computational advancements such that it is possible to understand the structure of even the most complex molecular systems, such as, proteins. One community derives information from average atomic charge densities from X-ray data and the other from valence orbital electron densities based on vibrational spectroscopy data. The modern generation of synchrotrons and the powerful free electron lasers (X-FEL) offer new opportunities and exciting challenges in structural science, but they will require a coordinated approach of complementary methods if they are to achieve maximum impact. We are constantly improving technical and computational methods to accelerate and automate characterisation processes and this is crucial to the fields to be explored in this meeting.

This Faraday Discussion will bring together world experts in computational, crystallographic, spectroscopic, chemical, biological and numerous characterisation methods to share and enhance their expertise.

Aims

The main aim for this FD is to bring together crystallographers and spectroscopists from chemistry, physics and biology to promote new interdisciplinary research and to benefit from complementary approaches and techniques in the rapidly emerging areas of 'time resolved studies', leading to a greater overall understanding of structural dynamics.Â

We hope to achieve:Â

• cross-fertilization of recent knowledge in time and length scales
• linking structural and dynamical information (derived from both the techniques) to understand function
• understanding non-equilibrium states and their impact on reactivity
• new collaborations towards solving problems jointly. Â

In addition, the discussion meeting is expected to identify future challenges and the novel techniques yet to be developed towards addressing temporally and spatially resolved structure-function relationships in chemistry and biology.Â

Format

The Faraday Division have been organising high impact Faraday Discussions in rapidly developing areas of physical chemistry and its interfaces with other scientific disciplines for over 100 years.Â

Faraday Discussions have a special format where research papers written by the speakers are distributed to all participants before the meeting, and most of the meeting is devoted to discussing the papers. Everyone contributes to the discussion - including presenting their own relevant research. The research papers and a record of the discussion are published in the journal Faraday Discussions.Â

Themes

• Dynamics of the Chemical Bond New experimental and theoretical approaches to understand chemical bonding and the changes that take place in the excited state for a number of biologically and technologically important reactions. Obtaining insights into and recording data from processes associated with changes to chemical bonds, whether that is bond breaking, formation, changes in length or inter-/intra-molecular vibrations, is key to obtaining further understanding of a wide range of chemical and biological reactions.
• Time and Space Resolved Methods Development and exploitation of high resolution time-resolved crystallographic and spectroscopic methods predominantly for reactions occurring in the solid-state and examining processes occurring on a broad range of timescales (ms-fs), including novel methodologies and interdisciplinary approaches which are transferable to the study of a wide range of molecular processes. Combining structural, spectroscopic and theoretical data (in 1D, 2D or 3D) within the reaction energy landscape/surfaces will provide complementary information and give a more complete picture of the underlying the behaviour of chemical reaction or biological process.
• Local and Global Dynamics Understanding the relationship between local and global dynamics is essential to correlate knowledge of a molecular process to those occurring within an extended structure e.g. whether a process is cooperative and affected by the surround lattice or occurs independently of the local environment. A combination of current and emerging experimental and theoretical approaches, most of which are transferable between disciplines, will be discussed to provide maximum insight into the relationship between structure and function for both chemical reactions and biological processes.
• Future Challenges and Emerging Techniques Exciting new directions for combining time resolved spectroscopic and diffraction techniques with modern theoretical approaches and looking forward to how we can exploit lab sources to XFELs in novel ways, bringing together all of the topics and ideas covered in earlier sessions to define new research approaches and inter-disciplinary collaborations. Â

We look forward to welcoming you to Bangalore for this Faraday Discussion.

Symposium in the 87th Annual Meeting of the Japanese Biochemical Society

Various methods for structural studies, such as X-ray crystallography (PX), X-ray small angle scattering (SAXS), cryoEM and molecular simulation, have been evolved very rapidly in the last decade. Combinations of these techniques reveal dynamic aspect of the molecular mechanism of biological macromolecular complexes based on the atomic structures.

This symposium celebrates the International Year of Crystallography (IYCr) in 2014 and will highlight several recent results on structural studies on membrane proteins and huge protein complexes by X-ray crystallography together with recent advance of important techniques for structural life sciences.

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