Protein Crystallography Newsletter Volume 6, No. 5, May 2014 Crystallography in the news In this issue: May 3, 2014. A research team led by Professor Jennifer Potts, a British Heart Foundation Senior Research Fellow in York's Department of Biology, studied how Staphylococcus Crystallography in the news aureus attach to two proteins fibronectin and fibrinogen found in human blood. News: IUCr 23rd Congress May 4, 2014. Arizona State University scientists, together with collaborators from the Science video of the month Chinese Academy of Sciences in Shanghai, have published a first of its kind atomic level Upcoming events look at the enzyme telomerase that may unlock the secrets to the fountain of youth. Product spotlight: BioSAXS-2000 Crystallographers in the news May 7, 2014. Soon the Advanced Photon Source (APS) will get a boost in efficiency that likely will translate into a big boon for the discovery of new pharmaceuticals. The world's Scientist spotlight: Susan Buchanan first protein characterization research facility directly attached to a light source will open Useful links for crystallography in the near future at the APS. The Advanced Protein Characterization Facility (APCF) will Survey of the month use state-of-the-art robotics for gene cloning, protein expression, protein purification and protein crystallization. Recent crystallographic papers Book reviews May 12, 2014. Google honors Dorothy Hodgkin's X-ray vision with a molecular doodle. The event marks the 104th anniversary of the British chemist, who pioneered the use of X- rays to determine the structure of biological molecules. Special News Item IUCr 23rd Congress May 13, 2014. A key step in the decades-long mystery of the HIV life cycle was uncovered using what formerly was thought of as only a supplementary X-ray technique for structural biology. This advances study of HIV as well as highlights a powerful tool, Small Angle X-ray Scattering (SAXS), to obtain currently unobtainable high-resolution structural determination and characterization of RNA molecules. May 14, 2014. University of Missouri researchers have completed a 3-D map of an enzyme called Proline utilization A (PutA). PutA facilitates metabolism by adding oxygen to molecules. Biochemistry Prof. John Tanner says mapping this enzyme will give researchers a better understanding of its function, which could help drug manufacturers create more effective drugs. May 14, 2014. Scientists at La Trobe University published a study this week about a The Twenty-Third Congress and General Assembly of protein found in the flowers of ornamental tobacco plant that targets human cancer cells the International Union of Crystallography (IUCr 2014) and destroys them. This raises the prospect of the deepest kind of irony: tobacco grown will take place at the Palais des congrès de Montréal to produce drugs used to treat cancers caused by tobacco. from August 5-12, 2014. Located in the heart of Montréal, the Palais des congrès has gained an May 16, 2014. A new study reveals that a protein of the Ebola virus can transform into excellent reputation for its hospitality, superior services three distinct shapes, each with a separate function that is critical to the virus's survival. and functional flexible facilities. Each shape offers a potential target for developing drugs against it. May 22, 2014. A promising anticancer agent about to enter human clinical trials is on the Science Video hook because of a chemical structure error discovered by scientists at Scripps Research Scotch tape unleashes X-ray power by unrolling it in a vacuum Institute California. The patented compound, known as TIC10 or ONC201, is owned by the biotech firm Oncoceutics. However, Scripps has applied for a patent on the corrected structure and has licensed it exclusively to another company, Sorrento Therapeutics. May 24, 2014. MiTeGen LLC, a provider of innovative consumables for X-ray diffraction, crystallography and protein crystallization to academic, pharmaceutical, industrial and government researchers around the world, has been awarded a Phase II SBIR (Small Business Innovation Research program) award from the NIH (National Institute of Health) for the development of a rapid crystal cooling device ("hyperquencher") for cryocrystallography and other sciences requiring safe, controlled, high-speed cooling of samples. New product introduction: Rigaku BioSAXS-2000 Researchers at the University of California, Los Angeles, have shown that it is possible to produce X- Rigaku's new BioSAXS-2000 SAXS camera is designed specifically to rays by simply unrolling Scotch tape. In the journal Nature, Dr. Putterman and his colleagues report that meet the needs of the structural biologist and, with improved flux, surprisingly fierce flows of electrons were unleashed as now increases throughput for home lab experiments. the tape was unpeeled and its gooey adhesive snapped free of the surface. The electrical currents, in The BioSAXS-2000 is equipped with the new OptiSAXS optic, a turn, generated strong, short bursts of X-rays — each doubly focusing multilayer optic whose focus is at the detector. The OptiSAXS provides burst, about a billionth of a second long, contained better than two fold improvement in flux compared to it's predecessor resulting in higher about 300,000 X-ray photons. brilliance at the sample position and data collection times in the range of minutes. Thus, the BioSAXS-2000 brings a beamline experience to home laboratory SAXS experiments. Optional accessories include an Automatic Sample Changer (ASC) with support for 8 or 96 samples and the Automatic Analysis Pipeline (AAP) based on ATSAS, the world's most popular SAXS analysis software developed at EMBL Hamburg. Ask for more information. Lab spotlight: Susan Buchanan @ NIH Susan Buchanan, Ph.D. Principal Investigator, NIDDK Bethesda, MD 20892 Dr. Buchanan is Chief of the Section on Structural Biology of Membrane Proteins in the National Institute for Diabetes & Digestive & Kidney Diseases, at the National Institutes of Health. She received her Ph.D. from the Johann-Wolfgang-Goethe Universität in Frankfurt, Germany in 1990. She completed postdoctoral fellowships at the MRC Laboratory of Molecular Biology, Cambridge, UK, and at UT Southwestern Medical Center, Dallas, before returning to the UK to establish a research group at Birkbeck College, London in 1998. She joined the NIDDK as a tenure track investigator in 2001 and is currently a senior investigator in the Laboratory of Molecular Biology, NIDDK. The focus of her group's research program is the structure determination of integral membrane proteins by X-ray crystallography and functional analysis of these proteins using biophysical, biochemical, and cell biological techniques. They study transporters embedded in the outer membranes of Gram-negative bacteria, which are surface accessible and therefore have the potential to be good vaccine and/or chemotherapeutic New Rigaku BioSAXS-2000 targets against infectious diseases. They also study the membrane associated or soluble protein partners that interact with outer membrane transporters to better understand how these systems function in vivo. Current topics in the lab include [1] small molecule and protein import across the bacterial outer membrane, [2] protein secretion by pathogenic Crystallographers in the News bacteria, and [3] protein import across mitochondrial outer membranes. Crystallographers Elected Fellows of the Royal Society 2014 Professor Randy Read FRS, Wellcome Trust Principal Research Fellow, Professor of Protein Crystallography, Cambridge Institute for Medical Research, University of Cambridge. Professor Read is known internationally for his outstanding and fundamental contributions to the development of macromolecular crystallographic software. His application of maximum likelihood based algorithms to the solution of macromolecular crystal structures by molecular replacement (a technique that uses the known structure of a homologue to solve an unknown structure) has resulted in software (Phaser) that is foremost in the field. He also devised and demonstra - Useful link: DNAWorks (v3.2.2) ted an improved likelihood target function for model refinement that has been adopted by all major refinement programs. In addition, Professor Read has DNAWorks (v3.2.2) - Automatic oligonucleotide design for PCR-based gene synthesis. The led structural work that has made significant contribu - availability of sequences of entire genomes has dramatically increased the number of tions to understanding the mechanisms of proteins protein targets, many of which will need to be overexpressed in cells other than the relevant to disease (bacterial toxins and serpins). original source of DNA. Gene synthesis often provides a fast and economically efficient approach. The synthetic gene can be optimized for expression and constructed for easy mutational manipulation without regard to the parent genome. Yet design and construction of synthetic genes, especially those coding for large proteins, can be a slow, Professor James Naismith FMedSci FRS, Professor of Chemical Biology difficult and confusing process. DNAWorks automates the design of oligonucleotides for and Director of Biomedical Sciences gene synthesis by PCR-based methods. Research Complex, University of St Andrews. A description of DNAWorks can be found: (Hoover, D. and Lubkowski, J., 2002). Professor Naismith is cited for his stunning structural and chemical dissection of the many proteins involved in natural product recognition, synthesis