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.


Felix Frolow 1947-2014

[Felix Frolow]

Prof. Felix Frolow has passed away, Friday, Aug. 29th 2014.

Felix was a true scientist, not the one for PR or short cuts, but the one who always thrived to find the right answer. He was a scientist who knew structural biology in all its levels from the physics behind the X-ray machine and the science of X-ray crystallography, to the biological and chemical mechanisms behind the systems he was investigating.

For many years he worked at the structural biology department at Weizmann Institute, Rehovot Israel and then moved to build, from scratch, the X-ray Crystallography Laboratory at the Tel Aviv University, Israel, a lab he headed till his untimely death.

Felix was a good friend and colleague. He was an intelligent opinionated person; exchanges with him were never dull.

My deepest condolences to his wife and daughters.

He will be deeply missed.

Miri Hirshberg

Felix Frolow was a Co-editor of Acta Crystallographica Section D from 1997 to 2007, and was a Co-editor of Acta Crystallographica Section F from 2005 onwards. He will be greatly missed by the journals.

Posted 01 Sep 2014 


IUCr news digest 29 August 2014

closing ceremonyOver 2200 delegates from around the world came together in Montreal, Canada earlier in August to take part in the 23rd IUCr Congress and General Assembly. After years of planning and countless hours of work from the crystallographic community, the local organising committee and the international programme committee, delegates enjoyed a fantastic programme of lectures, meetings, workshops, poster sessions and other activities. Over eight packed days of events delegates were able to explore the latest advances in crystallography covering a broad range of scientific disciplines, from material and life sciences to chemistry and engineering. With an opening ceremony that included performances by Cirque Eloize, a Canadian entertainment company, the Congress was certainly a meeting we will all remember. A more detailed report will appear over the coming weeks on the IUCr website; we will notify all World Directory of Crystallography users who have opted in for alerts when it becomes available. Take this opportunity to sign up or refresh your account by visiting http://www.iucr.org/people/wdc so you will be one of the first to read the in-depth report. The 24th Congress and General Assembly will be held in Hyderabad, India from 21 to 29 August, 2017; you can visit the website http://www.iucr2017.org for further information. If you have any comments or ideas for the meeting, please get in touch - we’ll be pleased to hear from you.

littledictA Little Dictionary of Crystallography, edited by André Authier and Gervais Chapuis, was available for sale at the Congress and sold out within a few hours of the exhibition opening. Copies are now available at the special discounted price of 9 GBP, 11 EUR, 13.80 USD or your equivalent local currency. You can place your order by visiting http://tinyurl.com/little-dictionary. The 40% discount on the list price will remain for the duration of the International Year of Crystallography 2014.

One of the many exciting developments announced at the Congress was the launch of the IYCr2014 Legacy Fund. This fund will ensure that many of the activities taking place during the year such as initiatives in Africa, IUCr-UNESCO OpenLabs, summit meetings and other IYCr outreach events continue into 2015 and beyond. More information about the IUCr Legacy Fund and how you can contribute will be announced shortly on our website.

The First European Crystallography School is currently taking place in Pavia, Italy. The number of places available for students wishing to learn about the different facets of crystallography had to be more than doubled to cater for the unprecedented demand, you can find out more about the school by visiting the website http://ecs1.azuleon.org/ .

Finally for this digest, during the month of August our managing editor responsible for Acta Crystallographica Section C: Structural Chemistry ( http://journals.iucr.org/c/ ) attended the 248th American Chemical Society National Meeting and Exposition in San Francisco, CA, USA. It was an excellent meeting and we look forward to attending future events.

Posted 29 Aug 2014 


IUCr Executive Committee 2014-2017

[IUCr Executive Committee 2014-2017]

At the twenty third Congress and General Assembly of the International Union of Crystallography Professor Marvin L. Hackert was elected as the new President of the IUCr. The photograph shows the Convener of the Finance Committee and the Executive Secretary alongside Professor Hackert and the other members of the new Executive Committee for the triennium 2014-2017.

Back row: M. J. Cooper (Convener, IUCr Finance Committee), M. H. Dacombe (Executive Secretary). Executive Committee: J. M. Guss, R. Kuzel, M. Takata, W. Depmeier, S. Garcia-Granda. Front row: H. Dabkowska, L. Van Meervelt (General Secretary and Treasurer), M. L. Hackert (President), A. M. Glazer (Vice-President), G. R. Desiraju (Immediate Past President).

Please join the IUCr in welcoming the new Executive Committee and thanking those members retired.

Posted 21 Aug 2014 


Acta Crystallographica Section F: Structural Biology Communications

f_64At the recent IUCr Congress it was decided to improve the scientific quality of those articles published in Acta Cryst. F that relate to the crystallization of biological macromolecules. For an article to be accepted for publication it should describe more than just the routine crystallization of a macromolecule. Articles describing novel aspects of the crystallization procedure together with new science will be welcomed by the journal, and from 2015 all articles will be published in the category Research Communications. This enhancement should make the articles more relevant and useful to the structural biology community as a whole, and an editorial with further details will be published in the near future.

Posted 19 Aug 2014 

research news

The difficult question of Clostridium difficile

wa5073coverfigThe bacterium Clostridium difficile causes antibiotic-related diarrhoea and is a growing problem in the hospital environment and elsewhere in the community. Understanding how the microbe colonises the human gut when other "healthy" microbes have been destroyed during a course of antibiotics might lead to new ways to control infection. An important clue was reported recently in an open access article published in the journal Acta Crystallographica Section D Biological Crystallography. [Bradshaw et al. (2014). Acta Cryst. D70, 1983-1993; doi:10.1107/S1399004714009997]

Ravi Acharya of the University of Bath, UK, and colleagues have reported the first crystal structure of the C. difficile surface protein Cwp84. This cysteine protease enzyme is found on the surface of the bacterium and assists with production of the microbe's surface-layer, which is likely to play an essential step in the colonisation of the gut. The enzyme cleaves a single polypeptide (surface-layer protein A; SlpA) into low- and high-molecular-weight subunits. Now, Acharya and colleagues have identified three critical regions in a mutant of the enzyme that could represent novel targets for drugs to attack C. difficile by blocking maturation of its surface layer during colonisation.

While C. difficile can be present in the normal, healthy gut (3-5% of adults), when a patient requires treatment for infection with broad-spectrum antibiotics, other protective intestinal microbes are eradicated in the process and the incidence increases to about 20%. This leaves space for the pathogenic C. difficile to grow rapidly unhindered leading to the release of toxins that cause bloating, pain and severe diarrhoea. Sometimes potentially life-threatening pseudo-membranous colitis or toxic megacolon occurs (about 5 to 8% of patients). Outbreaks occur when people ingest the spores, often in contaminated medical facilities and C. difficile is known to kill tens of thousands of people every year worldwide. Mild cases are often resolved by simply halting antibiotic treatment but in more severe cases last-line antibiotics such as vancomycin and metronidazole are often needed. Worryingly, the relapse rate is 20 to 30%.

The team explains that while Cwp84 is essential for correct surface layer formation it may also break down extracellular proteins, such as fibronectin, laminin and vitronectin which are found in the body. Nevertheless, blocking its activity either genetically or chemically prevents proper growth of bacterial colonies even if this is not in itself bactericidal. Disruption of the colonization process might therefore be possible allowing healthy microbes to repopulate the gut and stifle the spread of C. difficile.

The researchers carried out X-ray crystallography at station I03 at Diamond Light Source in Didcot, UK. The resulting high-resolution (1.4 angstrom) diffraction data revealed the structure of the N-terminal propeptide, the cysteine protease domain, and a previously uncharacterized "linker" region that is 170 amino acids long. The linker lies between the cysteine protease domain and the repeat region of Cwp84 which holds it onto the cells surface. The linker region binds calcium and resembles a group of proteins known as lectins, so may have an affinity for carbohydrates which may be vital for correct cell wall processing. The same motifs are present in other types of Clostridium microbes as well as ancient single-celled organisms known as archaea.

The team suggests that the insights their research offers in terms of C. difficile surface layer growth and how this relates to gut colonization could be exploited in developing a new type of drug to treat infection-anti-colonization inhibitors.
Posted 18 Aug 2014


Dear Colleagues

We are very pleased to announce the launching of the Small Angle Scattering Biological Data Bank (SASBDB, www.sasbdb.org). SASBDB was developed in accordance with the plans of the wwPDB SAS task force to establish a federated system of interconnected databases for X-ray and neutron scattering (SAXS/SANS).

SASBDB is a curated repository that makes experimental SAS data and derived models of biological macromolecules discoverable, citable and downloadable. Within SASBDB, it is possible to browse the scattering data and models, search by various keywords including macromolecule name, buffer composition, experiment setup and author/affiliation details. 3D representations of low resolution ab initio bead models and of the hybrid rigid body models are available. All data sets and models can be freely downloaded.

Presently, SASBDB comprises of 96 experimental data sets and 151 models. Most of the entries contain published data from the studies where SAS was used for the structural analysis of macromolecular solutions (proteins, nucleic acids and complexes). There are also several "benchmark" data from a set of well-characterized commercially available proteins. The SAXS (and, for some proteins, also wide-angle scattering, WAXS) data from these samples were collected using an on-line purification system to ensure sample monodispersity. The benchmark set data and models can be used to test computational approaches, for tutorials etc.

Researchers are welcome to deposit the SAXS/SANS data and models into SASBDB (prior to or after the publication). The submission requires a simple sign-in procedure followed by filling in an on-line deposition form and uploading the data/models. ATSAS and ATSAS-online users may directly use their credentials to sign in. The deposition is pre-moderated, i.e. the entries will be validated before making them public.

ATSAS Team, EMBL-Hamburg
Posted 06 Aug 2014