Scientific Programme 

The meeting will consist of a mixed programme of scientific workshops and sessions from speakers from both industry and academia. A detailed scientific programme will be provided at the end of September

The scientific workshops will be taking place on the afternoon of the 12th of November. There will be workshops covering the following topics: X-ray Crystallography, Solution Based Studies (NMR, ITC, SPR, MS), Cryo-Electron Microscopy, Cryo-Electron Microscopy Scipion data processing tutorial (

The scientific sessions will start in the morning on the 13th of November and will finish by lunchtime on the 14th of November and will be attended by all meeting participants. In addition to the topics covered during the workshops, the scientific sessions will include talks covering Drug Design Case Studies, Membrane Proteins & Hot Structures, Fragment Based Drug Design and Emerging Techniques & Software.

12 November 2017 - Workshops & Welcome Reception

12:00 - 13:00 Registration Opens
13:00 - 14:45 Cryo-Electron Microscopy Workshop
Chair: Pamela Williams
X-ray Crystallography Workshop
Chair: Marc O'Reilly
13:00 - 13:30 Tom Ceska (UCB Pharma) Gerhard Klebe (University of Marburg)
13:30 - 14:00 David Barford (MRC Laboratory of Molecular Biology) Isabel Moraes (Membrane Protein Laboratory - Diamond Light Source)
14:00 - 14:45 Submitted and open questions Submitted and open questions
14:45 - 15:15 Coffee Break & Networking
15:15 - 17:00 Solution Based Methods Workshop
Chair: Glyn Williams
Scipion - Data Processing Tutorial for Cryo-EM
15:15 - 15:40 Sheena Radford (Astbury Centre - University of Leeds) Jose Maria Carazo (Instruct Image Processing Center in Madrid)
15:40 - 16:05 Alvar Gossert (ETH Zurich - Institute for Molecular Biology and Biophysics)
16:05 - 16:30 Natalia Markova (Malvern Instruments)
16:30 - 17:00 Submitted and open questions
17:00 - onwards Exhibitors Set-up (stands must be set up by 19:45 on 13 November at the latest
19:00 - 21:00 Welcome reception: drinks & canapes at the Fitzwilliam Museum
21:00 - onwards Delegates organise their own dinner arrangements

13 November 2017 - Scientific Meeting & Meeting Dinner

08:00 - 09:00 Registration & Coffee Station (Atrium Foyer)
09:00 - 09:15 Welcome Address
Harren Jhoti (Astex Pharmaceuticals)
09:15 - 10:00 Keynote Speaker
Chair: Harren Jhoti
  Tom Blundell (University of Cambridge)
10:00 - 12:50 Session 1 - Drug Design Case Studies
Chair: Tom Davies
10:00 - 10:25 Sandra Jacob (Novartis Institutes for Biomedical Research)
10:25 - 10:50 Andrew S Dore (Heptares Therapeutics Ltd)
10:50 - 11:20 Tea/Coffee Break, Exhibitors & Networking (Atrium Foyer & Suites)
11:20 - 11:45 Andrew Turnbull (CRUK Therapeutic Discovery Laboratories)
11:45 - 12:10 Rob Van Montfort (The Institute of Cancer Research)
12:10 - 12:20 Sponsor Talk: Cube Biotech GmBH
12:20 - 12:30 Sponsor Talk: Atum
12:30 - 12:40 Sponsor Talk: iNEXT
12:40 - 12:50 Sponsor Talk: Dectris
12:50 - 13:50 Lunch Break, Exhibitors & Networking
13:50 - 15:20 Session 2 - Cryo-Electron Microscopy
Chair: Judith Reeks
13:50 - 14:15 Peijun Zhang (eBIC-Diamond)
14:15 - 14:40 Neil Ranson (Astbury Centre)
14:40 - 14:50 Sponsor Talk: Formulatrix
14:50 - 15:00 Sponsor Talk: Arinax
15:00 - 15:10 Sponsor Talk: Molecular Dimensions
15:10 - 15:20 Sponsor Talk: Bruker AXS
15:20 - 15:50 Tea/Coffee Break, Exhibitors & Networking (Atrium Foyer & Suites)
15:50 - 17:55 Session 3 - Solution Based Studies
Chair: Reto Walser
15:50 - 16:15 Alex Breeze (University of Leeds)
16:15 - 16:40 Finn Holding (Astex Pharmaceuticals)
16:40 - 17:05 Christina Redfield (Department of Biochemistry, University of Oxford)
17:05 - 17:30 Carol Robinson (University of Oxford)
17:30 - 17:55 Mike Williamson (University of Sheffield)
18:30 - 19:30 Drinks Reception (Trinity Hall College - Graham Storey Room and Terrace Room)
19:30 - 23:00 Meeting Dinner (Trinity Hall College - Main Hall and Terrace Room)

14 November 2017 - Scientific Meeting

07:30 - 08:00 Coffee Break, Exhibitors & Networking (Atrium Foyer & Suites) 
08:00 - 10:20 Session 4 - Emerging Techniques & Software
Chair: Magdalini Rapti
08:00 - 08:25 Randy J. Read (University of Cambridge)
08:25 - 08:50 Justyna A. Wojdyla (Swiss Light Source, Paul Scherrer Institute)
08:50 - 09:15 Frank von Delft (Diamond Light Source)
09:15 - 09:40 Stephanie Monaco (ESRF)
09:40 - 09:50 Sponsor Talk: Rigaku Europe
09:50 - 10:00 Sponsor Talk: OpenEye
10:00 - 10:10 Sponsor Talk: BIOSAXS GmbH
10:10 - 10:20 Sponsor Talk: Chemical Computing Group
10:20 - 10:50 Coffee Break, Exhibitors & Networking (Atrium Foyer & Suites)
10:50 - 13:00 Session 5 - Membrane Proteins & Hot Structures
Chair: Dominic Tisi
10:50 - 11:15 E. Yvonne Jones (Welcome Trust Centre for Human Genetics - University of Oxford)
11:15 - 11:40 Jun Lu (Merck Research Laboratories)
11:40 - 12:05 Gunter Fritz (Institute of Neuropathology, University of Freiburg)
12:05 - 12:30 Chris Tate (MRC Laboratory of Molecular Biology)
12:30 - 12:45 Workshop Wrap-up
12:45 - 13:00 Concluding Remarks & Awards
13:00 - 14:00 Lunch break & dismantle exhibitor set-up

PSDI 2017 Invited Speakers

Keynote Speaker:
Sir Professor Tom Blundell
(University of Cambridge)

"Tom Blundell maintains an active laboratory as Director of Research and Professor Emeritus in Biochemistry, University of Cambridge, where he was previously Sir William Dunn Professor and Head of Department (1996 - 2009) and Chair School of Biological Sciences (2003 - 2009). He previously held teaching and research positions in the Universities of London, Sussex and Oxford.

Tom researches on molecular, structural and computational biology of growth factors, receptor activation, signal transduction and DNA repair, important in cancer, tuberculosis and familial diseases. He has described complex assemblies of FGFR and Met receptor systems necessary for high signal to noise in cell signalling, and of DNA double-strand-break repair, both NHEJ including DNA-PK and HR (Rad51 and BRCA2).

Tom has produced many software packages for protein modelling and design including Modeller (~9500 citations) and Fugue (~1300 citations), and for predicting effects of mutations on stability and interactions (SDM & mCSM) to understand genetic disease and drug resistance. He has published 595 research papers, including 35 in Nature and Science.

Tom developed new approaches to structure-guided and fragment-based drug discovery. In 1999 he co-founded Astex Therapeutics, an oncology company that had eight drugs in clinical trials when sold in 2013 to Otsuka for $886 million, and recently has a breast cancer drug FDA approved. In the University of Cambridge he has developed structure-guided fragment-based approaches to drug discovery for difficult targets involving multiprotein systems including Met receptor and Rad51-Brca2 complexes. He has targeted mycobacterial proteins as part with Gates HIT-TB and EU-FP7 MM4TB consortia.

Tom was a member of PM Margaret Thatcher’s Advisory Council on Science & Technology (1988-1990), Founding CEO of Biotechnology and Biological Sciences Research Council, 1991-1996 (Chair 2009-2015), Chairman, Royal Commission on Environment (1998-2005), Deputy Chair of Institute of Cancer Research 2008-2015 and President of UK Science Council, 2011- 2016."

Dr Randy Read
(University of Cambridge) 

"I obtained my BSc (1979) and PhD (1986) degrees in Biochemistry from the University of Alberta in Edmonton, Canada, where I learned protein crystallography from Michael James. After a post-doctoral fellowship with Wim Hol at the University of Groningen in The Netherlands, I returned to the University of Alberta in 1988 to take up a faculty appointment in the Department of Medical Microbiology & Immunology. In 1998 I moved to the University of Cambridge in the UK, where I was appointed as Professor of Protein Crystallography in the Department of Haematology. Since 2008 I have chaired the X-ray Validation Task Force for the worldwide Protein Data Bank, which developed the criteria underlying the validation reports now provided for every entry in the PDB. In 2014 I was elected to the Royal Society of London.

My group combines the development of new methods for solving crystal structures with the study of proteins that give structural insight into pathogenesis. Our work on methods concentrates on the application of maximum likelihood to crystal structure solution by either molecular replacement (in which the known structure of a homologue is rotated and translated to provide an initial atomic model of the crystal) or single-wavelength anomalous diffraction (applicable to novel structures). We find that the use of likelihood can dramatically enhance the power of these methods, which are implemented in our program Phaser available through the CCP4 and Phenix packages. Our work on structure determination has focused recently on two major themes: enzymes mutated in inherited metabolic diseases, and non-inhibitory members of the serpin family of proteins, particularly those involved in carriage or production of hormones."


Professor Gerhard Klebe
(University of Marburg)

Focus of our research is directed toward the understanding of protein-ligand interactions, including chemical synthesis, microcalorimetry, molecular biology, crystallography, bioinformatics and software development. Internationally recognized software tools such as CoMSIA, AFMoC, DrugScore, Relibase/Cavbase or MOBILE have been developed in our laboratory. Several drug discovery projects concentrate on the discovery of leads for neglected and poverty-related disease targets. To obtain better insight into affinity and selectivity determining features fundamental research is performed on serine and aspartyl proteases, aldose/aldehyde reductase and several kinases and hydrolases. Gerhard Klebe studied chemistry at the University of Frankfurt/M, Germany, and obtained his doctorate in physical chemistry. After postdoctoral positions in crystallography (Grenoble, CNRS and ILL, France, and Univ. of Berne, Switzerland) he was responsible for molecular modeling and crystallography at BASF-AG in Ludwigshafen, Germany. In 1996 he moved to Philipps-University of Marburg, Germany, to take a professorship in Pharmaceutical Chemistry. In 2005 he refused an offer from ETH Zürich, for a chair in Pharmaceutical Chemistry, serves on the editorial board of several journals, was member of the Board of Governors of the CCDC and the advisory board of the Leibniz-Institute FMP in Berlin. He has written a text book on Drug Design which appeared either in the German and English language. In 2011 the research of his group was awarded an ERC Advanced Grant by the European Research Council on the “Chemogenomic profiling of drug-protein binding by shape, enthalpy/entropy and interaction kinetics” with particular emphasis to understand the influence of water on ligand binding. Presently, his groups installs together with scientists at Bessy, HZB Berlin, a crystallography-based fragment screening beamline facility. From his group more than 350 scientific papers and about 900 PDB entries have emerged. He organized in two years frequency an International Workshop on New Approaches in Drug Discovery and Design.


Dr. Chris Tate
(MRC Laboratory of Molecular Biology)

Chris Tate is a membrane protein biochemist with extensive experience of expression, purification and structure determination of transporters and G protein-coupled receptors. He obtained his PhD in Bristol (1989) and then moved to the Biochemistry Department in Cambridge to work on bacterial sugar transporters. He subsequently obtained a Postdoctoral Research Fellowship at Girton College to work at the LMB on the structure determination of the cocaine-sensitive serotonin transporter, with a back-up project on the structure determination of the multidrug transporter EmrE. It was through working with both very stable and unstable transporters that led to the idea of developing a generic process for the thermostabilisation of membrane proteins to facilitate their structure determination. This resulted in the process of conformational thermostabilisation, a technique to thermostabilise membrane proteins in a specific conformation by scanning mutagenesis coupled to thermostability assays, and culminated in the structure determination of a number of GPCRs, such as the β1-adrenoceptor, the adenosine A2A receptor and the neurotensin receptor. This technology was used as the basis to found the drug discovery company Heptares Therapeutics in 2007, which uses the thermostabilisation technology to develop drugs to GPCRs by structure-based drug design. More recently, a thermostabilised mini-G proteins was developed that has allowed the structure determination of of the adenosine A2A receptor in the fully active state.


Dr Natalia Markova
(Malvern Instruments)

"Natalia Markova has a PhD in Analytical Chemistry from University of Chemical Technology, Ivanovo, Russia and a PhD in Physical Chemistry from University of Lund, Sweden.

Natalia has extensive experience in academic and industrial applications of differential and isothermal microcalorimetry, thermal analysis, dynamic light scattering, analytical ultracentrifugation and surface plasmon resonance.

During the last 14 years she worked in Drug Discovery and biopharmaceutical development as Senior Scientist at Structural Chemistry department of Biovitrum AB, Head of Biophysics at the Structural Genomics Consortium, Karolinska Institute, Associate Director of Biophysical facility in a contract research organization iNovacia AB in Stockholm, Sweden and Senior Customer Relation Manager at

GE Healthcare Life Sciences.

In 2014 Natalia joined Malvern Instruments where she continues working on the development and applications of label-free technologies as Principal Scientist – MicroCal and Leader – Scientific Marketing Bioscience."


Dr Rob van Montfort
(The Institute of Cancer Research)

"Rob van Montfort joined the Institute of Cancer Research (ICR) in London in 2007 where he set up high-throughput X-ray crystallography to support drug discovery at the Institute’s Cancer Research UK Cancer Therapeutics Unit and was crucially involved in setting up the Unit’s fragment screening capabilities.

He is currently leading the Unit’s Hit Discovery and Structural Design (HDSD) team, which is responsible for hit generation using high-throughput and fragment-based approaches for projects in the Unit’s portfolio. The HDSD team informs the Units drug discovery projects using a variety of cell-based and biochemical assays as well as with biophysical techniques such as isothermal titration calorimetry, surface plasmon resonance and X-ray crystallography.

Previously he worked at Astex Therapeutics in Cambridge, where he was involved in fragment-based drug discovery using X-ray crystallography and nuclear magnetic resonance (NMR).

He received his PhD in protein crystallography at the University of Groningen, the Netherlands and has worked as a postdoctoral fellow at the School of Crystallography at Birkbeck College, University of London.

Together with the team leaders from the Cancer Research UK Cancer Therapeutics Unit and the Royal Marsden Hospital’s Drug Development Unit he was awarded the 2012 team science award from the American Association of Cancer Research."


Professor Sheena Radford
(University of Leeds)

Sheena graduated in Biochemistry at Birmingham, completed her PhD at Cambridge, and then carried out extensive research at Oxford before becoming a lecturer at the University of Leeds in 1995, rising to become Director of the Astbury Centre in 2012. She became the Astbury Professor of Biophysics in 2013.

Her research is focused on fundamental structural molecular biology, specifically the measurement of the conformational dynamics of proteins and the elucidation of the role that these motions play in protein folding and misfolding in health and disease. She and her group are using a wide range of biophysical methods (including NMR, mass spectrometry and single molecule methods), to determine how proteins fold in all-atom detail; the mechanisms by which proteins misfold; and the complex macromolecular assemblies associated with some of the deadliest human diseases.

Sheena has published more than 250 peer-reviewed papers and has given 360 invited lectures at national and international meetings, including more than 200 invited lectures at international conferences in twenty countries. She has successfully supervised 45 postdoctoral researchers and 57 PhD students, and follows their subsequent careers with interest: these include significant numbers of academic, research and industrial posts, and technical and journal editing.

She has served on numerous grant panels, scientific advisory boards and editorial boards, and continues to have an active role in these.

Sheena has won various prizes, including the Biochemical Society Colworth Medal and the Protein Society Carl Brändén Award. She is a Fellow of the Royal Society of Chemistry, the European Molecular Biology Organisation, the Academy of Medical Sciences, and the Royal Society."


Dr Stephanie Monaco

After a PhD at EMBL-Grenoble with S. Cusack and in collaboration with BioMérieux (Lyon) on structural studies of human HIV-1 P24 in complex with a Fab using crystallography, Stéphanie Monaco-Malbet did a post-doc at ESRF on yeast Sec12p with S. Wakatsuki. For the last 15 years, she has been the ESRF liaison for industrial clients at ESRF in structural biology. She is also strongly involved in the automation of the structural biology beamlines at the European Synchrotron, adapting to the evolution of the field and building new features responding to industrial demands.


Dr Alvar Gossert
(Institute for Molecular Biology and Biophysics)

"Alvar Gossert studied biochemistry at ETH Zürich (Switzerland) and completed his PhD in the laboratory of Prof. K. Wüthrich at ETH Zürich as well. For his postdoctoral studies, he joined the Novartis Institutes of BioMedial Research where he was later hired as laboratory head. After 10 years with different roles at Novartis, he moved to ETH Zürich where he is now heading the NMR platform of the biology department.

Alvar Gossert’s interests lie in advancing research on biological systems in collaboration with biologists of different areas, by applying NMR technology. His lab focusses on technology developments in the fields of isotope labelling – with emphasis on labelling in eukaryotic cells – and NMR experimental techniques to study molecular interactions, from simple binding characterization up to structure determination of protein-ligand complexes."


Dr Isabel Moraes
(Membrane Protein Laboratory - Diamond Light Source)

Since 2010 Isabel Moraes is the Group Leader for the Membrane Protein Laboratory (MPL) at Diamond Light Source that is funded by the Wellcome Trust. The laboratory is a user facility for research and training in structural biology of membrane proteins. Isabel has been responsible for management of the facility as well as its scientific research. She provides scientific advice and guidance to all the projects at the MPL. In addition, Isabel is resposible for the stablishment of internal and external collaborations (national and international). She has been collaborating with the Diamond MX beamline scientists regarding to the development of new methodologies in crystallisation and structural determination of membrane proteins, including prototype systems for high throughput methods, improving handling of small and delicate crystals and methods for collecting and merging data from a large number of small crystals. In the last years Isabel has participated and organized many courses and workshops in field of membrane protein structural biology in the UK and abroad. Previously to MPL she worked as a structural biologist in industry where she gained vast experience in drug discovery. Her PhD degree and postdoctoral position were also in structural biology applied to drug discovery projects in collaboration with industry. Isabel is also involved in the use of X-ray free electron lasers (X-FEL) in the field of membrane protein structural biology.


Professor Alex Breeze
(University of Leeds)

Professor Alex Breeze holds the Chair of Biomolecular NMR in the Astbury Centre for Structural Molecular Biology and the Faculty of Biological Sciences at the University of Leeds, UK. He is Director of NMR in the University’s Astbury BioStructure Laboratory, and was formerly a Principal Scientist at AstraZeneca R&D, Alderley Park, UK. After a PhD at Imperial College London and postdoctoral research in the lab of Professor Iain Campbell FRS at the University of Oxford, Alex joined the then ICI Pharmaceuticals (later Zeneca, then AstraZeneca) in the early 1990s to establish the Biomolecular NMR Group, applying advanced NMR spectroscopy techniques in drug discovery programmes against a wide range of protein targets, chiefly in the oncology and anti-infectives areas. He pioneered the adoption of fragment-based approaches using NMR against a number of challenging drug targets, work that has led to clinical candidates from fragment start-points. In Leeds, his research focuses on the structural molecular biology and therapeutic inhibition of proteins of biomedical relevance, particularly those involved in cellular signalling and epigenetics, cancer metabolism, and trypanosomal infections.


Professor E. Yvonne Jones
(Welcome Trust Centre for Human Genetics - University of Oxford)

Prof E. Yvonne Jones is Joint Head of the Division of Structural Biology and Acting Director of the Wellcome Trust Centre for Human Genetics at the University of Oxford. Over the last 20 or so years she has developed a programme of research into the structural biology of cell surface receptors and signalling assemblies. Her current research aims to integrate high resolution mechanistic detail with lower resolution cellular context and is focused on cell guidance cues, cell adhesion receptors and Wnt signalling.


Professor Christina Redfield
(Department of Biochemistry, University of Oxford)

Since obtaining a Ph.D in Chemistry from Harvard University in 1984, Prof. Christina Redfield has pursued a research career in biomolecular solution-state NMR spectroscopy at the University of Oxford. Her research focuses on the application of state-of-the-art NMR techniques to the study of protein structure, function, dynamics and folding. Proteins studied include lysozyme, interleukin-4, alpha-lactalbumin, EGF-domain containing fragments (from fibrillin, fibulin, LTBP, Notch and CRB1), the thiol-disulfide oxidoreductase DsbD, the cytochrome c maturation protein CcmE, and the response regulators CheY3 and CheY6. In these studies, particular emphasis is placed on using NMR to obtain information not available from static X-ray structures. This includes the characterisation of both fast and slower timescale backbone dynamics, the determination of functionally important pKa values and the study of partially folded proteins.


Professor Peijun Zhang
(University of Oxford)

Dr. Peijun Zhang obtained her Ph.D. in molecular physiology and biophysics from University Virginia, M.S. in physics and B.S. in electrical engineering from Nanjing University, China. She was a postdoc and later a staff scientist at the National Cancer Institute, NIH. In 2006, she joined the faculty at the University of Pittsburgh School of Medicine as an assistant professor, and was promoted to associate professor with tenure in 2012. She recently joined the University of Oxford, and as the director of eBIC (the UK National Electron Bio-imaging Centre) at the Diamond Light Source, UK. Her scientific program aims at an integrated, atomistic understanding of the molecular mechanisms of large protein complexes and assemblies by developing and combining novel technologies for high-resolution cryoEM and cryoET with complementary computational and biophysical / biochemical methods. In particular, her lab continues to focus on two exciting and important biological systems: i) HIV-1 pathogenesis, in particular HIV-1 capsid assembly, maturation, and interactions with host cells; ii) Mechanisms of signal transduction and transmission in bacterial chemotaxis response. Dr. Zhang received many awards, including the Carnegie Science Emerging Female Scientist Award, Senior Vice Chancellor’s Award, United States Department of Health and Human Services “On-the-Spot” Award.


Dr Finn Holding
(Astex Pharmaceuticals)

Finn Holding studied for his PhD whilst working at the Public Health Laboratories at Porton Down prior to joining Cantab Pharmaceuticals in 1995 as an Analytical Scientist to develop HPLC and MS based methods to analyse protein immunotherapeutics. He moved to Astex pharmaceuticals in 2002 where he has been the protein mass spectrometrist and has grown the mass spec platform to enable analysis of proteins and protein ligand complexes to inform the various stages of the drug discovery process.

Professor Mike P. Williamson
(University of Sheffield)

Mike Williamson did a degree and PhD in Chemistry at Cambridge, then went on to research fellowships at Cambridge (with Dudley Williams) and at ETH Zürich (with Kurt Wüthrich). He worked for 6 years at Roche in Welwyn Garden City, on a wide range of drug development projects, and then moved to the Department of Molecular Biology and Biotechnology at the University of Sheffield, becoming a Professor in 2001 and Head of Department in 2017. While with Wüthrich, he determined the first globular protein structure to be solved by NMR. He co-authored a book on the Nuclear Overhauser Effect (NOE) with David Neuhaus, and has developed methods for calculating and using chemical shifts in proteins. These have been applied (among other things) to study the behaviour of proteins at high pressure. He has also worked on proline-rich regions in proteins; carbohydrate-binding domains and their interactions; salivary proteins and polyphenols; the bacterial light-harvesting complex; DNA-binding drugs (inicluding binding to DNA quadruplexes); and methods for detecting salt bridges in proteins. He has also written an undergraduate textbook on proteins.


Professor Frank von Delft
(Diamond / U.Oxford SGC)

Frank has been head of the PX group since the start of the SGC in 2004, focussing on methodology and high-throughput techniques for protein crystallography. In late 2012 he joined the Diamond Light Source synchrotron as head of beamline I04-1. In this role he is working to make Fragment Screening by X-ray Crystallography an easily accessible and routine experiment for both academic and industrial users.

Frank received his undergraduate degree from the University of the Free State (Bloemfontein, South Africa), and gained his PhD in protein crystallography under Tom Blundell at Cambridge (UK). He has also worked as a postdoc in San Diego (academically at Scripps in the JCSG, industrially at Syrrx in its pre-Takeda days). He is a visiting professor at the Biochemistry Department of the University of Johannesburg.


Dr David Barford
(MRC Laboratory of Molecular Biology)

David Barford studied for his D.Phil in Louise Johnson’s group at the Laboratory of Molecular Biophysics at Oxford University investigating the structural consequences of protein phosphorylation on the allosteric enzyme glycogen phosphorylase. In 1991 he moved to to Cold Spring Harbor Laboratory to establish an independent research program on protein phosphatases. In 1994 DB returned to the University of Oxford as a lecturer and fellow of Somerville College, and in 1999 was appointed as the co-head of the Division of Structural Biology at the Institute of Cancer Research in London. He moved to the MRC Laboratory of Molecular Biology in Cambridge in 2013. There his group is interested in using recent advances in single particle electron cryo-microscopy to determine the atomic structures of functional states of the APC/C.

  Other Invited Speakers   
  Dr. Sandra Jacob  (Novartis Institutes for Biomedical Research)
  Professor Dame Carol Robinson

 (University of Oxford)
  Dr. Tom Ceska  (UCB Pharma) 
  Professor Neil Ranson  (University of Leeds)