|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 International Union of Crystallography (IUCr) is seeking an Executive Secretary to lead the organization, and to manage its day-to-day operations.
The IUCr is a Scientific Union and publisher. It is governed by a General Assembly that meets every three years; between these meetings the work of the Union is delegated to the Executive Committee. The Executive Secretary reports to the Executive Committee through the General Secretary.
The IUCr has offices in Chester, UK, and employs 25 staff, chiefly in its publishing operations. The successful candidate is expected to manage the financial and administrative affairs of the Union, as well as having responsibility for the staff.
The successful applicant will have a science degree or PhD, ideally with experience of international collaboration in science, and a good knowledge of English. The ability to handle financial matters such as overseeing the preparation of the annual accounts by external accountants and dealing with taxation and investment matters is required. As well as dealing with the general administration of the Union (50 Adhering Bodies and 23 Commissions), the successful applicant will be expected to take a proactive role in raising the profile of the IUCr and crystallography, and directing its educational and outreach programmes.
Strong attention to detail and networking ability are a must, and experience of project management will be beneficial. A competitive salary is offered (£50,304 - £61,453; exceptional candidates may be appointed at a higher grade) with excellent benefits. You will be based in Chester and expected to undertake overseas travel.
To apply for the position, send a CV, names of two referees, and a covering letter to Mike Dacombe (email@example.com) by 30 September 2016.
Neutron radiography is a non-destructive imaging technique, which provides information about the interior of an object with high spatial resolution by using neutron radiation. In contrast to X-ray radiography, neutron imaging is sensitive to some light elements such as hydrogen or lithium, while most heavy elements such as, for example, lead and aluminium can easily be penetrated. Consequently, this method is routinely applied in fields such as cultural heritage research, materials science, engineering, and geology, whenever X-rays fail to generate sufficient imaging contrast or lack penetration.
Nowadays, spatial resolution down to 50 microns are routinely obtained by means of neutron imaging, which are limited by the geometric resolution of the beamline and the resolution obtainable with neutron detectors. Several approaches have been proposed to investigate smaller structures. They are either based on the direct magnification of the image by focusing neutron optics or on the improvement of the detector resolution. However, if a direct resolution is not required, even smaller structures can be studied by a spatially resolved mapping of their scattering signature. A complementary imaging approach based on this principle is provided by neutron grating Interferometry (nGI).
Simply, nGI is an advanced neutron imaging method which allows the simultaneous recording of the neutron transmission image, the differential phase contrast image and the dark–field image.
The improving theoretical understanding of the nGI contrast mechanism has recently triggered the transition of nGI towards a quantitative method providing detailed information about the microstructure of the sample.
In a recently published paper in the Journal of Applied Crystallography, a group of scientists [Reimann et al., (2016). J. Appl. Cryst. 49, doi:10.1107/S1600576716011080] report on the setup and applications of a new neutron grating interferometer which has recently been implemented at the ANTARES imaging beamline at the Heinz Maier-Leibnitz Zentrum (MLZ).To learn more about ANTARES and to apply for beamtime visit this page.
A number of activities involving or relevant to crystallography took place at the recent International Data Week in Denver, Colorado. A session on Crystallography and Structural Data Bases explained to a general audience how some of the world’s foremost research databases maintain and deliver access to the enormous research value of their individual high-quality curated resources. The experience of the crystallography community in creating an interoperable workflow spanning experiment, software analysis, journal publication and database deposition and dissemination was described in a session on Building a Disciplinary, Worldwide Data Infrastructure. The specific experience of the IUCr as a sponsor of the Crystallographic Information Framework was highlighted in the session Coordination of Data Management Policy and Practice across ICSU Unions/Disciplines in an Open Data World. The IUCr position paper for crystallography in response to the Science International Accord Open Data in a Big Data World was presented to the CODATA Gemeral Assembly and very favourably received. The IUCr also participated in the General Assembly of the International Council for Scientific and Technical Information (ICSTI) and in various sessions of the 8th Research Data Alliance Plenary Meeting. Learn more in our report.John R. Helliwell, U. Manchester (IUCr Representative to CODATA)
In the past decade there have been huge improvements in
synchrotron sources, instrumentation at macromolecular crystallography (MX)
beamlines, X-ray detectors, and data-processing and structure-determination
software. These have led to an unprecedented increase in the number of
These developments have also called for a revision of data-collection practice for single crystals. Hybrid photon-counting (HPC) pixel-array detectors have revolutionized data collection, both in terms of speed and in terms of quality. They offer several novel features including single-photon sensitivity, a sharp point-spread function of one pixel, millisecond and noise-free readout, and a high dynamic range. HPC pixel-array detectors can enable shutterless data collection, improving the data quality and reducing the data-acquisition time.
A recent paper by the MX group at the Swiss Light Source, published in Acta Cryst. D [Casanas et al., (2016), Acta Cryst. D72, 1036-1048; doi:10.1107/S2059798316012304] describes the best way of collecting macromolecular diffraction data with an EIGER HPC detector. In collaboration with DECTRIS, the group has integrated a DECTRIS EIGER and shown that it can be used to measure higher quality data than some earlier detectors. This has been enabled by features like the virtually continuous sensitivity of the detector for X-rays, only interrupted by microsecond breaks for the readout, enabling optimized data acquisition schemes at high speed and single photon accuracy.
The EIGER detector series is considered to represent the current state of the art of X-ray detectors for synchrotron and laboratory applications. Its development has widened the range of applications from high resolution data collection to experimental phasing and serial crystallography and allowed crystallographers to determine structures of more complex biological molecules, and this in turn can increase our understanding of their role in health and disease processes.
The benefits of open access for readers are clear but authors also benefit as articles have increased visibility, are more widely read, are cited sooner and achieve higher citation rates. Currently, two of the nine IUCr Journals are fully open access, i.e. all articles are made available free of charge to the reader, and the remaining seven include a mix of open-access and subscription-only articles.
Further information about open access at IUCr Journals can be found at http://journals.iucr.org/services/openaccess.html.
The IUCr has been an early adopter of open access and is also delighted to be an early adopter of the new Wellcome Trust publisher requirements.
Water plays a substantial role in the fundamental events of biological processes and regulates biomolecular structure and dynamics in living cells. Interactions with water are demonstrated to be critical for protein structure, flexibility and folding. It has also become increasingly clear that water molecules play an active role in a number of protein-dependent functions. Because proteins are the central players in cellular activities it is of vital importance to understand protein-water interactions.
X-ray crystallography is one of the tools used to determine the positions of water molecules within proteins at atomic resolution. With the continuous evolution of X-ray sources, detectors, software and protein engineering techniques, very high resolution crystal structures are now routinely available.
A group of scientists from the US [Gupta et al. (2016), J. Synchrotron Rad. 23. 1056-1069; doi: 10.1107/S1600577516009024] discuss how the method of synchrotron X-ray radiolytic labelling mass spectrometry (XF-MS) can be used to directly distinguish the interactions of bulk and bound water with protein side chains in solution. With this technique, the scientists are able to demonstrate how reactive hydroxyl radicals are generated in situ by high-flux-density X-rays, causing covalent labelling of protein side chains which were detected by mass spectrometry. The in situ covalent labelling approach eliminates most of the complexity associated with sample preparation necessary with other high-resolution techniques and at the same time allows easy comparative structural analysis of protein samples under various physiological relevant conditions.
For the past decade, XF-MS has been integrated effectively with many other structural and biochemical techniques to provide a comprehensive picture of macromolecular complexes and their functional states. The XF-MS method offers a new tool for optimising ligand design by mapping the location and the thermodynamic properties of water molecules at protein binding sites and, at the same time, XF-MS data can be used to develop, validate and refine molecular dynamics approaches that determine water-protein side-chain interactions.
Another exciting future application is the use of X-ray footprinting for protein crystallography, which could yield valuable information in several important areas. Currently dedicated XF-MS beamlines are under development at both the ALS and NSLS II. These beamlines are designed for fully automated sample handling, microsecond irradiation timescales and time-resolved experiments, and will open the door to even further advances in the techniques of XF-MS.