Welcome to the

International Union of Crystallography

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.

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IUCr Associates Programme goes live

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Join the IUCr Associates Programme and become part of the IUCr and a growing network of crystallographers. The IUCr is involved in many charitable activities including supporting students to attend meetings around the world, a Visiting Professor scheme and building crystallography capacity in Africa and other parts of the world.

The Associates Programme offers a series of benefits and tools to help you network, share ideas and discover more about crystallography, benefits include

  • Discounts on the open-access fee for publishing an article in an IUCr journal
  • A number of free article downloads from IUCr journals
  • Discounts on books from other publishers such as Wiley and Oxford University Press
  • Professional networking opportunities, such as access to the IUCr LinkedIn discussion group and job listings
  • Resources to help in your professional development

To learn more about the Associates Programme please follow this link.

A 20% launch discount is currently available on the three-year joining fee of USD 200 (USD 160 with the discount). A reduced rate of USD 60 (USD 48 with the discount) is available for students, retired scientists and those from developing countries.

Take advantage of this limited-time discount by joining now.

If you have any questions about the Associates Programme please get in touch by emailing us at associates@iucr.org or by submitting your query via this web form.

Posted 02 Nov 2017 

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IUCr Publications

A new section of the IUCr website highlights IUCr publications, past and present. It provides a convenient interface for reaching online journals and International Tables content, and for ordering books published by the IUCr or in association with other publishers. We invite you to browse this new section, which appears in the new design that will be progressively applied across the IUCr website in the coming months.

Posted 02 Nov 2017 

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GigaFRoST: the gigabit fast readout system for tomography

pp5108A thorough understanding of dynamic processes in areas as diverse as biomechanics, materials science miniature engineering, and energy research relies on our ability to observe structural changes of materials in three-dimensional detail at high speeds. X-ray microtromography is a technique capable of looking inside opaque objects without destroying them. So far, the observation of very fast processes has been hindered by the lack of suitable camera systems. To enable live time-resolved measurements of real dynamic phenomena over extended periods of time, a group of scientists in Switzerland [Mokso et al. (2017), J. Synchrotron Rad. 24, 1250-1259] have developed a new high-frame-rate camera readout system, called GigaFRoST (Gigabit Fast Readout System for Tomography).

While a number of commercial imaging systems are capable of acquiring images with very high frame rates, they are usually designed for burst operation, storing data on internal memory which is read out only after the measurements and at speeds much slower than the experiment duration. This results in essentially blind acquisition. Moreover, the total acquisition time is limited by the size of the available memory, which is usually not enough to cover the full duration of a dynamic process. GigaFRoST solves this problem by streaming the data from the camera directly to a dedicated server, which is able to make the data available for previewing and analysis essentially in real time, while the amount of data that can be acquired is limited only by the server memory or the attached file storage capacity.

This advancement opens up countless new opportunities for the observation of dynamic systems with high temporal resolution, such as crack propagation in materials, bubble growth in metal foams, musculoskeletal motions in insects, and many more.

Making use of a modular and easily extendable, parallelizable architecture, the same data streaming approach can be used and adapted for other high-performance detector systems.

Dr Christian M. Schlepütz
Beamline Scientist, Paul Scherrer Institut, Switzerland
Posted 08 Nov 2017 

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IUCr bursary case study: custom-designed supramolecular materials

daltonIn 2016 alone, the IUCr sponsored 40 international meetings and schools. One recent recipient of an IUCr Young Scientist Award describes the importance of these grants to their research and experience.

Custom-designed supramolecular assemblies have been an area of intense research because of their potential applications in a wide range of disciplines within the chemical and material sciences. Substantial progress has been made from the exploration of a range of heterotopic chelating ligand species, due to their favourable metal-binding properties and modular syntheses. The polypyridine family of ligands is often exploited in coordination chemistry due to their coordination behaviour, and the favourable electronic and magnetic properties of the resulting complexes. These complexes have found applications in dye-sensitized solar cells, redox photocatalysts, molecular magnetism and spin-crossover devices. My project involves the development of unsymmetrically substituted 2,2´-bipyridine scaffolds and incorporation into coordination polymers  and supramolecular materials and the investigation of their structural, photophysical and mechanical properties as well as the self-recognition processes governing their formation. The knowledge obtained from single-crystal X-ray data will allow an understanding of the coordination environment of these systems which will then be applied in the design and engineering of metallosupramolecular assemblies. In addition, the aim will be to use this functionalised bipyridine motif to generate tripodal systems with a view to forming supramolecular materials such as amorphous polymers or gels.

The IUCr bursary allowed me to travel to the BCA/CCG Intensive Teaching School in X-ray Structure Analysis in Durham. The school, where you have professors and lecturers at your disposal, provided invaluable knowledge in the mathematics, physics and chemistry which underpin X-ray diffraction as a technique. Through lectures, tutorials as well as interactive learning the intensive school covered each aspect and allowed me to gain an understanding to progress and apply this learning in a practical way moving forward in my career. As well as the content it delivered, it also gave me the opportunity to meet other students, post-docs and academics in the same field. The hospitality was incredible and everything from the accommodation to the food was fantastic.

Hannah Dalton, PhD student, Trinity College Dublin, Ireland
Posted 24 Oct 2017 

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Ted Janssen 1936-2017

janssen2017On 29 September 2017, Emeritus Professor T. W. J. M. (Ted) Janssen passed away at the age of 81 years. Together with Aloysio Janner he was one of the founders of the superspace approach in crystal-structure analysis for the description of quasiperiodic crystals and modulated structures. Ted was a Co-editor for Acta Crystallographica Section A from 1993 to 2002, and was awarded the Aminoff prize of the Royal Swedish Academy of Science (with P. M. de Wolff and A. Janner) in 1988 and the tenth Ewald prize of the  International Union of Crystallography (with A. Janner) in 2014. Ted was highly respected for his ability to combine a deep knowledge of physics with a rigorous mathematical approach, and his work with Janner had a huge impact on the development of crystallography. He will be sorely missed by his many friends and colleagues in the crystallographic community. A full obituary will be published in due course.
Posted 13 Oct 2017 

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2017 Nobel Prize for Chemistry

nobel winners chemistry 2Richard Henderson, recent winner of the International Union of Crystallography (IUCr) Gjønnes Medal in Electron Crystallography and IUCrJ editorial board member, has been awarded the 2017 Nobel Prize in Chemistry with Jacques Dubochet, and Joachim Frank "for developing cryo-electron microscopy (cryoEM) for the high-resolution structure determination of biomolecules in solution".

In 1995, Henderson published a rigorous theoretical analysis of the potential of cryoEM of single particles to determine atomic resolution structures of randomly oriented macromolecules. He identified key barriers to progress, particularly the need to develop better electron detectors and improved computer programs for single particle image analysis. These methods, particularly the development of new direct electron detectors with higher detection efficiency, have revolutionized cryoEM as a mainstream structural biology tool, exemplified by IUCr’s decision to launch a cryoEM section in its premier journal IUCrJ.

Professor Samar Hasnain, Editor-in-Chief of IUCr Journals commented, “Henderson continues to lead in the development of cryoEM by helping to solve remaining barriers, namely (a) the need for higher detector DQE, (b) the need to reduce beam-induced specimen charging and motion, and (c) the deleterious effect of interaction of biological macromolecules with the air-water interface during plunge freezing”.

Professor Hasnain went on to say, “Henderson’s vision and ability to identify and solve key problems while focussing on an important biological problem has transformed cryoEM, which has been adopted by X-ray based structural biologists around the world”.

In August 2017 Richard delivered his Gjønnes medal lecture at the 24th Congress and General Assembly of the IUCr in Hyderabad, India. A video of his talk entitled “From electron crystallography to single particle cryoEM” can be viewed here.

You can see a full list of IUCr papers published by Richard Henderson by clicking here.

You can see a full list of IUCr papers published by Joachim Frank by clicking here.

Picture credit: MRC Laboratory of Molecular Biology, Columbia University Medical College, AP
Posted 04 Oct 2017