In this issue:

• Crystallography in the news
• Crystal imaging for protein crystallography
• Upcoming crystallography meetings
• Webinar: tips and tricks for getting funded
• Useful links for crystallization
• Selected recent crystallographic papers
• FAQ: screening with UV imaging
• Survey question of the month

Continuing Education Webinar Tips and Tricks for Getting Funded What's Hot and What's Not Presenter: Dr. Joe Ferrara April 23 at 2:00 PM EDT (18:00 GMT) Click here to register

Crystallography in the news

March 6, 2009. Researchers use crystallography to uncover a common weak point in flu virus strains that could lead to universal flu vaccines. Listen to the NPR interview with Professor Ian Wilson of Scripps.

March 18, 2009. University of Illinois at Chicago research on understanding the structure of membrane proteins may lead to more effective treatment of infections. The research team is looking at proteins called multidrug resistance transmembrane efflux pumps.

March 19, 2009. Researchers at the University of Liverpool and the MRC Prion Unit at University College London may have uncovered a clue, using protein crystallography, that could help treat a family of rare progressive neurodegenerative disorders that includes CJD, which is closely linked to Mad Cow Disease.

Crystal imaging for protein crystallography

Automatically image crystallization experiments and link images with crystallization conditions with the affordable Rigaku's Desktop Minstrel™ system. Data is captured in CrystalTrak™, a complete virtual crystallization laboratory, which provides a chemical and crystallization database, data analysis tools, and methods for easily designing optimization and initial crystallization screens. Additionally, CrystalTrak Web uses web browser technologies to provide remote viewing over the web or across other platforms such as Mac/OS or LINUX®.

Using a high-resolution imaging system that can visualize hanging drop, sitting drop, microbatch, and interface diffusion experiments across most commercially available plate types, the Desktop Minstrel facilitates scoring and reporting, as well as experimental design and project management. This cold room compatible system is modular and expandable with the addition of a 160-plate capacity Gallery™ 160 Plate Hotel. The Desktop Minstrel can provide unattended scheduled image acquisition, ensuring that no crystals are missed and providing an objective history of the experiment. All Rigaku crystal imaging and crystallization systems are engineered and manufactured in California, USA with an ISO 9001 certification.

Request a copy of the Desktop Minstrel brochure.

Webinar: tips and tricks for getting funded

The new Rigaku Life Sciences Webinar Series continues on April 23rd with a discussion on grant funding. Presented by Joseph D. Ferrara, Ph.D., this complementary webinar will review tactics for getting funded. Click here to register.

Useful links for crystallization

Cryoprotection of delicate crystals, in 2 easy steps (and 16 hard steps). Artem G. Evdokimov (2006). This paper summarizes, in great detail, one novel approach for difficult crystals.

XtalPred is a neat web application for the prediction of protein crystallizability. In part, the program provides a summary of protein features and predictions that indicate problems that are likely to be encountered during protein crystallization.

Selected recent crystallographic papers

High-throughput screening: designer screens. Nathan Blow. Nature Methods, 6, 105-108 (2009).

Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data. W.N. Price, Yang Chen, S.K. Handelman, H. Neely, P. Manor, R. Karlin, R. Nair, J. Liu, M. Baran, J. Everett, S. N Tong, F. Forouhar, S.S. Swaminathan, T. Acton, R. Xiao, J.R. Luft, A. Lauricella, G.T. DeTitta, B. Rost, G.T. Montelione and J.F. Hunt. Nature Biotechnology, 27, 51-57 (2008).

Crystal structure of human prion protein bound to a therapeutic antibody. S.V. Antonyuk, C.R. Trevitt, R.W. Strange, G.S. Jackson, D. Sangar, M. Batchelor, S. Cooper, C. Fraser, S. Jones, T. Georgiou, A. Khalili-Shirazi, A.R. Clarke, S.S. Hasnain and J. Collinge. Science, 323, 396-401 (2009).

FAQ:  screening with UV imaging

With the advent of modern imaging technologies and crystallization tools, researchers are able to rapidly create hundreds and thousands of experiments. Screening through those images can be a time consuming and daunting task. Visible images can often show objects that require close observation to determine if they are protein crystals or just precipitate or other matter. UV imaging allows researchers to screen through thousands of images much more rapidly and reliably, as they can simply look for the resulting fluorescence detected on the CCD and depicted in the image itself. For quantitative observation, the visible image can then be reviewed, thus eliminating the need to look through every visible image. UV Microscopy is a major advance over previous visible light microscopy approaches because its ultraviolet fluorescence (UVF) technology allows researchers to easily distinguishing protein crystals from non-protein crystals (such as salt).

The Desktop Minstrel™ UV from Rigaku offers a "Comparative Imaging" feature that provides simultaneous observation at both UV and visible wavelengths. This allows researchers to obtain immediate confirmation if an object is composed of protein (versus a salt crystal) and to employ the system in a high-throughput screening mode. Users, screening through UV images for "hits," can concurrently examine the visible wavelength image to check crystal quality, size, orientation, etc.

Request more information on a UV upgrade.