|The IUCr is an International Scientific Union. Its objectives are to promote international cooperation in crystallography and to contribute to all aspects of crystallography, to promote international publication of crystallographic research, to facilitate standardization of methods, units, nomenclatures and symbols, and to form a focus for the relations of crystallography to other sciences.|
The IUCr has initiated a major project to extend and expand the scope of its journals to meet the needs and serve the interests of researchers in the crystallographic and wider scientific communities who obtain and utilize structural information for addressing their scientific questions. The Editor-in-Chief, Samar Hasnain, appointed in August 2012, in consultation with appropriate committees and commissions of the IUCr, as well as with the wider structural science community, has developed an ambitious plan for IUCr journals. Its aim is to make the journals the natural home for many of the high-quality scientific publications that are currently published in journals such as Nature Structure and Molecular Biology, Structure, Proceedings of the National Academy of Sciences, Journal of the American Chemical Society, Angewandte Chemie, Chemical Communications, etc., where structural data underpin these publications. The overall development plan was approved by the IUCr Executive Committee in December 2012.
Chemists, biologists, physicists and material scientists will be actively encouraged to report the best of their structural studies in IUCr journals. Significant changes are being implemented in journal organization and management to coincide with the celebration of the International Year of Crystallography (IYCr2014). Major scientific advances require multidisciplinary research and very often these breakthrough papers report results covering a wide range of methods and technologies. The wide-ranging expertise that exists on our editorial boards is being further strengthened by appointing additional research leaders in chemistry, crystal engineering, biological sciences, materials science, free electron laser science and technology, and a broader range of structural methods so that our journals continue to lead in all aspects of structural science and methods. Subtitles of the journals in the Acta Crystallographica series are being changed to make it clear that we are open to publishing a wider range of science in these journals. The first issue of Acta Crystallographica B under its new subtitle Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials appeared on 1 February 2013, with other sections of Acta expected to follow soon.
Since crystallographic studies are critical to understanding the structural basis for chemistry, physics, biology and materials science, the IUCr will launch a new journal as part of the celebrations of IYCr2014. The new journal will be simply called IUCrJ. It will be fully open access, striving to reach the high impact and influence appropriate for the best of our structural sciences. Our aim is to capture high-profile papers on all aspects of the sciences, technologies and methods supported by the IUCr via its commissions, including emerging fields such as 3D structures from 'single molecules' using free electron lasers. Many of the exciting structural science results that have been published in other high-profile journals appeared first in presentations at IUCr congresses, and at AsCA, ECM and ACA meetings. The goal for 2014 will be to publish 100 articles in IUCrJ; many of these articles will be solicited from the presentations of cutting-edge research at ACA, ECM, AsCA meetings as well as the IUCr congress and conferences closely linked to IUCr via its Commissions. IUCrJ is thus intended to be a natural home for reporting breakthroughs and 'full' science reports rather than simply reporting structures and how they were determined.
A Management Board has been appointed including the Main Editors of the current journals and representatives of the IUCr Executive and Finance Committees. The board is responsible for: (a) increasing the influence of IUCr journals among the wider scientific communities; (b) serving the interests of all of its Commissions in its journals; (c) broadening the scope of the journals so that high-quality science papers that use crystallography are attracted to the journals; and (d) improving the visibility of IUCr journals at non-crystallographic conferences.
A Business Development Manager will be appointed in early 2013 with a mandate to (a) reach out to the wider science community, (b) encourage closer integration of the journals with the Commissions, (c) develop social media marketing, (d) boost article citations by writing press releases highlighting the most significant papers, (e) prepare market research reports including citation and usage trend analysis, (f) identify subject trends and new journal opportunities, (g) identify target authors and encourage them to submit to the journals, and (h) exploit opportunities arising from IYCr2014. The Business Development Manager will work closely with the editorial staff.
One of the most beloved and influential figures in the development of protein crystallography, Guy Dodson passed away peacefully on Christmas Eve, with his wife Eleanor and other family members at his side. Guy was an inspirational scientist whose engaging personality and passion for science have enriched the lives of many people round the world. Like many others I consider it a personal privilege to have known him.
Guy was born in Palmerston North, New Zealand, a small provincial city he liked to describe, affectionately, as 'the centre of the universe'. His secondary education was at Dilworth College, a small Auckland school with a mission to 'support, educate and train' boys from disadvantaged backgrounds. Whether Guy was ever 'trained' is debatable but there he and his twin brother Maurice - with whom he remained very close all his life - acquired a love of sport, history and science, together with a healthy disregard for authority.
Guy's love of crystallography and the concept of 'seeing molecules' came as a student at the Auckland University College. On attempting to enroll in history (his first choice), he was faced with a late enrolment fee of £10 - so chose chemistry instead. His career shows how fortunate that choice was, but he remained passionate about history; his Churchillian orations are legendary! Luckily, he found in Auckland an excellent crystallography research group, and undertook the X-ray analysis of a plant alkaloid as his PhD topic. He remained very grateful for the freedom he was given by his tolerant supervisor, David Hall, who gave guidance, support and crystallographic training while turning a blind eye to the impromptu cricket, water fights, fire extinguisher episodes
Guy's move to Oxford in 1962, when he went to work with Dorothy Hodgkin on what was originally expected to be only a short-term postdoctoral position, transformed his life. The revolution in the development of protein crystallography was gathering pace, and he became Dorothy's right-hand person in the successful solution of the structure of insulin, achieved in 1969. He also met and married Eleanor and fully embraced the Hodgkin philosophy of allowing individual talent to mature.
I came to Oxford in 1967, barely knowing what a protein was and somewhat overawed (should I wear a tie to the laboratory?). Guy's reaction was typical, warm and welcoming - definitely no ties! My initial brief was to develop data collection strategies on the new four-circle diffractometer, but I became absorbed into the insulin team, socially and scientifically. Guy and Dorothy shaped my whole approach to science, just as Guy was to do for many others later, making me feel that it was important, exciting and fun and best of all that I could do it! I went back to New Zealand full of confidence.
Guy remained in Oxford until 1976 when Dorothy retired. These were exciting days as the biology of insulin began to be teased out. It was already apparent that the hexameric 2Zn structure did not give all the answers, but many insulin biologists and clinicians came through the laboratory, and there were many 'aha!' moments when visitors would suddenly see the structural basis for some aspect of insulin behaviour.
Guy was sometimes asked 'what will you do next?' His answer was 'I haven't finished with insulin yet - there are so many interesting variations to explore'. This determination to understand insulin's conformational flexibility and complex biology has been richly vindicated: several billion-dollar drugs in the form of both rapid-acting and long-lasting insulin derivatives, developed by Novo Nordisk in collaboration with Guy's group; and most recently a
In 1976 Guy and Eleanor moved to York (where Maurice was already a lecturer in Mathematics) to set up a new laboratory in the Chemistry Department. The move surprised many, as they could have stayed in Oxford, but it was to bring the full flowering of both their talents. Their warmth of personality and large network of friends brought a steady stream of visitors, many of whom found a place in their cavernous home at 101 East Parade. You never knew who would appear for breakfast.
When I arrived with my wife Heather and our family to spend a year (1977-78) in York, the laboratory was very small, just three people. My experience, however, illustrates how it would develop. In New Zealand I had solved the structure of a cysteine protease, actinidin. Guy's structural and crystallographic instincts suggested this as a perfect vehicle for attempting to refine a protein structure from scratch by least squares. Eleanor's genius for crystallographic methods, which led to her later becoming the central figure in the CCP4 initiative, made it possible, and I was the beneficiary - it was a turning point in my career. I remember vividly the Saturday when we realised the refinement was working, sitting in York Minster listening to Handel's Messiah and thinking about the
Towards the end of our year, Guy was invited to Łódź, in Poland, to visit a group of young researchers wishing to establish research in protein crystallography there. He suggested I go, given my experience of doing the same in New Zealand. Ultimately this brought a series of talented Polish researchers to York, who enriched the York laboratory and expanded the Dodson 'family'. Guy's enthusiasm and openness, his generosity of spirit, and his willingness to devote his time to assisting and advising others, similarly attracted many more researchers to the York laboratory, making it a powerhouse in structural biology. Some stayed, to establish their own research programs, others moved on and made outstanding careers elsewhere. Thinking about how the York laboratory grew, it is clear that Guy was ambitious for good science, but not necessarily to do it all himself; he was very happy to enjoy the efforts of others.
As Dorothy Hodgkin had also done, Guy established effective collaborations with industry, on protein engineering, insulin derivatives and industrially useful enzymes. In 1993, Guy was persuaded to also lead a Division at NIMR in Mill Hill, where his energies established yet another internationally leading research group, bringing structural insights to biomedical research. In taking this position, he could not resist the lure of the biological research being undertaken at NIMR, and went on to play a major role in research projects dealing with malaria, TB and the structure of prions.
Guy had a broad vision. In addition to his insulin work, he conducted insightful studies of the mechanisms of action of haemoglobin and a variety of hydrolytic enzymes: penicillin acylases, amylases and lipases. His greatest delight came as he explored the exquisite beauty of catalytic sites, perfectly oriented hydrogen bonds and strategically placed water molecules. He was a tireless advocate for pursuing protein structures at the highest possible resolution, believing that key details of their chemistry would be revealed, but he also came strongly to the view that other approaches would provide complementary information, most notably molecular calculations.
Although he avoided the formalities of administration and undergraduate teaching as much as he could - in the process generating some legendary stories - he committed his full reserves of energy and persuasion into matters he thought were important for the community at large. As Chair of the IUCr Commission on Biological Molecules he led the way in establishing criteria for the deposition and release of both the data and the coordinates for biological structures, driven by the belief that they should be available to all. He campaigned tirelessly on issues such as the location of the Diamond Synchrotron and the NIMR. His wisdom and lack of personal agendas saw him widely sought as a reviewer and a PhD examiner. He had very high standards, but he understood human fallibilities.
Guy liked to say that he had never grown up, and there is some truth in this. He retained a boyish enthusiasm, and his love of life was infectious. He could be describing the exquisite beauty of the catalytic triad in serine hydrolases one moment and be bowling tricky leg-spinners down the laboratory corridor the next. A typical comment from a young researcher in my laboratory sums up his personal legacy: 'Though I met him only a few times I was always struck by his passion for both life in general and science in particular, as well as what I saw as a mischievous twinkle in his eye and his approachableness. I always came away from talking to him with renewed enthusiasm'.
Guy always saw the best in people, and as a result he got the best from them. Today, researchers all round the world, from the UK and Europe, to North America, Cuba, India, China, Australia and New Zealand - including Zbyszek Dauter and I, joint editors of Acta Crystallographica Section D - carry the benefits of their associations with Guy and an abiding and affectionate love for him.
The full obituary is also published in Acta Crystallographica Section D: Biological Crystallography.
University of Auckland, New Zealand
We announce with great sadness the untimely death of Roger Fourme, who played an important role in the advancement of synchrotron radiation research and was one of the founding co-editors of the Journal of Synchrotron Radiation.
Roger Fourme first enrolled into a curriculum for training school teachers, but his professors soon convinced him to switch to university studies in physics. After he obtained his PhD in this discipline, he became Assistant Professor at the University of Créteil near Paris, then Full Professor at the Université Paris XI, Orsay, in the late 1970s. There he joined the LURE synchrotron, which he soon placed in a prominent position on the international map of macromolecular crystallography and where he later acted as Head of the Biology Department. In the late 1990s he became an enthusiastic advocate of the construction of the French third-generation synchrotron, SOLEIL. He was one of its Science Directors until he retired in 2007, after which he continued working at SOLEIL as an Emeritus Professor. Roger has published extensively in the IUCr journals, including Acta Crystallographica (pre-1970), Acta Crystallographica Section B and Section D, Journal of Applied Crystallography and Journal of Synchrotron Radiation. He was a founding co-editor of the latter, reflecting his extensive reach into the field of synchrotron crystallography for life sciences in Europe.
Roger did not believe in grabbing the limelight for himself, but was tireless in pursuing avant-garde developments that could benefit the whole field as much as possible. Many who crossed paths or worked with him over the years recalled this after we learned of his untimely death on Christmas Eve at the age of 71, while he was skiing with his sons and grandchildren. Gérard Bricogne, for instance, says "it was Roger's unique enthusiasm, his radiant optimism, and his faith in how much could be achieved by simply pulling one's own sleeves up, that convinced me to take up a staff position within the French CNRS at the LURE synchrotron, which led to my long-term collaboration with him".
Roger's scientific contributions are concentrated in the area of experimental phase determination by means of anomalous scattering, in which his name is inseparable from that of his friend Richard Kahn who also died prematurely in the very recent past. Roger had an acute sense of the importance of establishing ties between people, which led to many collaborative projects in the development of innovative methods and instrumentation. This is exemplified by his joint exploration with George Charpak (long before Charpak won the Nobel Prize for Physics in 1992) of the potential of spherical-drift multiwire chambers as detectors for macromolecular crystallography data collection. The first version of this detector became available at LURE in 1980 (Mark I, known to many as Penelope), equipped with a computer interface that allowed macromolecular crystallography data collection with a tunable synchrotron beam. This enabled Roger and Richard to collect what is arguably the first MAD dataset ever on an unknown protein, namely a terbium derivative of a parvalbumin from Opsanus tau. The crash of a PDP cartridge unfortunately led to the loss of the primary images, and the structural results had to be derived from the reduced data as produced by the software current at that time, so that the final publication of this work in 1985 failed to do justice to its pioneering aspects [FEBS Lett. (1985). 179, 133-137]. By that time the commissioning of the much improved Mark II Charpak detector had been completed, and the challenge of providing it with software that could realise the full potential of that masterpiece of instrumentation led Gérard Bricogne to organize the European Economic Community (EEC) Collaborative Workshop on Position-Sensitive Detector Software from 1986 to 1989. This 'EEC MADNES' programme was pivotal in enabling this unique instrument to deliver MAD data of outstanding quality, as was demonstrated when LURE hosted Wayne Hendrickson and Bill Weis in 1991. They carried out a four-wavelength MAD experiment at the Ho edge on crystals of a mannose-binding protein, and obtained experimental phases of extraordinary precision [Science (1991). 254, 1608-1615]. This seminal work demonstrated that traditional heavy-atom complexes could be generally amenable to the MAD phasing method. At about the same time, Roger and Jack Johnson beat the resolution record for a virus crystal with a lattice dimension exceeding 1000 Å, further expanding the scope of synchrotron radiation [J. Appl. Cryst. (1984). 17, 147-153]. Roger also demonstrated that the noble gas xenon could be used for phase determination in protein structures [J. Appl. Cryst. (1994). 27, 950-960]. The method soon found itself in the limelight through its decisive role in the determination of the first structure of the ligand-binding domain of a nuclear receptor [Nature (1995). 375, 377-382]. Roger recently recalled that Richard and he had successfully implemented a set-up for cryogenic cooling as early as 1975, although this remained unpublished.
|Roger during the IUCr Conference on Advanced Crystallography at High Pressure, 2009, Harbin, China||Roger lecturing|
Roger's tendency to be self-effacing about his own achievements was not a sign of timidity: he could be an equally tireless and formidably persistent campaigner when he felt that he was defending the scientific community. These two sides of his personality worked together to remarkable effect in the well known 'Affaire du Synchrotron' in 1999-2000, when Roger undertook to fight a ministerial decision to cancel the previously fully approved and funded construction of the SOLEIL synchrotron. A key element in the success of this campaign was an open letter sent to Le Monde by Max Perutz who powerfully argued in favour of the SOLEIL project, following which a review process was set up that eventually led to the reinstatement of the SOLEIL project. Max Perutz's willingness to defend SOLEIL came in no small measure from his appreciation of Roger's deep and selfless commitment to the development of synchrotron radiation as a resource for macromolecular crystallography. This appreciation went back to an episode, some 20 years earlier, recounted by Max Perutz in his autobiographical book Science Is Not A Quiet Life, in which Roger had shown up at 3 a.m. during a visit to LURE by him and his post-doc Boaz Shaanan, just to make sure that everything was running well for their high-resolution data collection on deoxy-haemoglobin. This spontaneous act of support, going well beyond the call of duty, amplified through Max Perutz's gratitude and combined with Roger's own tenacious efforts within the campaign for SOLEIL, played a decisive role in enabling a new generation of multi-disciplinary synchrotron radiation research to take place in France.
Roger Fourme led the organization for the International Symposium for Diffraction Structural Biology (ISDSB) held in 2010 at the Université Paris Sud, and the location of the original French synchrotron facility LURE. ISDSB 2010 was the third such event. This was the first time though that the ISDSB was held outside Japan and also which newly added the electron and X-ray imaging tomography fields to the ISDSB subjects' range. The ISDSB conference series originated in Japan with the initiative led by the 169th committee of the University-Industry Cooperative Research Committee of the Japanese Society for the Promotion of Science (JSPS). The Paris 2010 event hosted by Roger has succeeded to give the ISDSB conference series worldwide popularity by the success of his organization.
Roger's subsequent scientific interests moved on towards macromolecular crystallography under high pressures and towards exploring the potential of ultra-short-wavelength X-rays in producing higher-quality diffraction measurements [J. Appl. Cryst. (2012). 45, 652-661]. It is a testimony to the visionary approaches of Roger that his recent work on the use of high-pressure crystallography to explore the conformational states of proteins made use of a diamond-anvil high-pressure cell which he first described in his PhD thesis article [J. Appl. Cryst. (1968). 1, 23-30], in which single crystals were maintained under high pressure (1-30000 bar) at adjustable temperature (293-493 K).
Roger knew how to transmit the sense of the freedom that can be enjoyed if one does science for the pleasure of seeing it progress through the work of a whole community, rather than nervously watching one's own list of personal publications in high-impact journals. His friend in politics, François Périnet, recalls that when he asked Roger what research needed in order to thrive, Roger used to answer 'freedom, serenity and time'. Roger never forgot that his family was from a modest background, and this is probably why he tirelessly worked towards the dissemination of knowledge and education to the majority of the population rather than to a privileged élite. This was reflected in his strong political commitment towards education for peace in the world, for which he travelled the planet with his wife Josette. He will be remembered as a man of outstanding talent, generosity, tolerance and passionate convictions.
The full obituary is also published in Journal of Synchrotron Radiation.Jacqueline Cherfils, Thierry Prangé, John R. Helliwell, Nori Sakabe, Michèle Sauvage, J. Friso van der Veen, SOLEIL Directorate and Editorial Board
Following the success of the inaugural virtual issue on polymorphism in December 2011 (http://journals.iucr.org/special_issues/2011/polymorphism/ ), Acta Crystallographica Section C is pleased to release its second virtual issue, which is on the topic of absolute structure (http://journals.iucr.org/special_issues/2012/absolutestructure/ ).The unambiguous determination of absolute structure, particularly where the absolute configuration of an enantiomerically pure chiral molecule is needed, is important not only for synthetic and natural-product chemists, who wish to fully characterize their products, but can be a critical step for the pharmaceutical industry, where opposite enantiomers of a drug can have quite different biological properties. One should also mention those crystal engineers endeavouring to prepare non-centrosymmetric crystals for applications such as second-harmonic generation.
A major impetus in enabling the study of absolute structure has been the advent of dual radiation CCD diffractometers. This means that more laboratories have routine access to Cu Kα radiation with the potential to successfully study light-atom structures. The latter have been viewed as one of the remaining difficulties in this field.
For the validation of absolute-structure determination, over the years there has been a heavy reliance on the statistics (values and standard uncertainties) of derived parameters or something equivalent, and little study of the fit of the model to the observed quantities. There has been little questioning of the quality of crystals, data collection and correction methodologies. Clearly, absolute-structure determination is still a rich field, wide open for development, especially for light-atom compounds of great importance to the pharmaceutical and chemical industries.
The concept of virtual issues of Section C is an initiative designed to make it easier for readers to find papers relevant to their field of interest, thus increasing the visibility and impact of those papers, and consequently the attractiveness of the journal to authors. This virtual issue has the ambition to present the results of crystal-structure determinations which demonstrate new successes and remaining limitations in absolute-structure evaluation.
The editors of Acta Crystallographica Section C hope that readers find this virtual issue interesting and beneficial. The next virtual issue, on the subject of metal-organic frameworks, will be published in late 2013.Anthony Linden
The Nobel Prize in Chemistry for 2012 has been awarded to Robert Lefkowitz (left, Howard Hughes Medical Institute and Duke University Medical Center, Durham, NC, USA) and Brian Kobilka (right, Stanford University School of Medicine, Stanford, CA, USA) for groundbreaking studies of G-protein-coupled receptors (GPCRs).
GPCRs allow the cells to sense their environment and respond to stimuli. They are responsible for many signalling processes, including the regulation of heart rate and blood pressure and the sensations of sight, smell and taste, and about half of all prescription drugs target GPCRs.
The mechanism of action of GPCRs at a molecular level was elucidated using X-ray crystallography. GPCRs are membrane proteins and as such are difficult to crystallize but once this hurdle was overcome the structure of activated receptors was solved and the mechanism revealed.
Former General Secretary and Treasurer of the IUCr and the Chair of the Nobel Committee for Chemistry, Professor Sven Lidin, has commented on the award as follows:
This year's Nobel Prize in chemistry celebrates the elucidation of the details of intercellular signalling. It rewards a number of important discoveries that together have given us an insight into the wonderful world of G-protein coupled receptors. Is this chemistry? Is it not biology or even medicine? The answer is that thanks to scientific contributions such as these, an important part of biology and medicine is chemistry today.
This Prize rewards work that is the natural continuation of the 1962 Nobel Prizes in Physiology or Medicine and in Chemistry. The now iconic structure of the DNA molecule and the groundbreaking work on the structure of globular proteins heralded a new era where structural biology has become an integral part of modern biochemistry.
Crystallography has come a very long way in 50 years, and it is continuously reinventing itself, allowing us to study problems that were unthinkable just a few years ago. Thanks to this development chemistry is becoming more crystallographic, as crystallography has become one of the necessary techniques for all chemists. Simultaneously, crystallography itself is becoming more chemical. The crystallization technique needed to ultimately solve the structure of a ternary complex in its active form is a scientific tour-de-force of unusual proportions. The receptor itself is designed to be flexible and the active complex is designed to be unstable and Brian Kobilka had to use every tool in the box, including several that he invented specifically for this purpose, to achieve crystallization.
For a list of articles on GPCRs published in IUCr journals please click here
A critical development which enabled the crystallographic work on this complex system was the microcrystallography. This enabled samples to be scanned to locate strong diffraction or to find small crystals, as well as data collection strategies to be developed that reduced scattered background and matched the beam to the diffracting volume. These aspects have been reported in the following articles in IUCr Journals:
For more details see the IUCr Nobel Prizewinners page.
Photo credits: (l.) Duke University Photography; (r.) Linda A. Cicero/Stanford News Service.
This is to communicate the excellent news that the United Nations has declared that 2014 will be the official International Year of Crystallography.
The initiative had been proposed by the International Union of Crystallography and spearheaded by the Moroccan Crystallographic Association.They have worked closely with the Permanent Representative of the Kingdom of Morocco in the United Nations along with helpful support from a number of delegations to the United Nations from other countries. The IUCr thanks the Moroccan authorities for the help and cooperation extended to us in bringing this proposal to fruition.
The declaration of IYCr 2014 provides all of us with a wonderful opportunity to sustain and renew our commitment to this outstanding subject. It has brought us together, whether we consider ourselves as crystallographers, or as physicists, chemists, biologists and materials scientists who work extensively with crystallography and its related techniques.
Ours is a very old subject, which shifted its emphasis from a study of crystals to a study of structures over a hundred years ago. Today, the subject is poised towards a study of dynamics and properties. All healthy scientific endeavour can recreate and reinvent: crystallography is a meaningful example of this.
I would like each and every one of you to use this opportunity to stimulate and ignite an interest in crystallography amongst students, scientists and the general public.
The declaration of IYCr 2014 by the United Nations is the finest endorsement for a subject that has weathered time and tide and continues to thrive. It signifies that crystallography has continuing cultural relevance and, in the end, this is the only justification for carrying out science in this rapidly changing world with its political and social flux and constant economic variables.
I will write about IYCr 2014 in more detail in the IUCr Newsletter but, in the meantime, I would ask all of you to participate in this happy occasion.Gautam R. Desiraju