X-ray crystallography and SAXS
Complementing the expertise of our X-ray Core, described below, are Dr. Peter Cherepanov, at The Francis Crick Institute in London, and Dr. Yong Xiong at Yale University. As a member of the PCHPI, Dr. Cherepanov is working to understand the structures of retroviral intasomes. Dr. Xiong is developing tools to understand the structure of the HIV-1 capsid in complex with various host factors that are known to bind the capsid.
co-Directors: Angela M. Gronenborn and Guillermo Calero, with Ying Wu as manager.
The X-ray Core is responsible for 1) refining crystallization and additive screens for protein complexes to optimize the probability of obtaining diffracting crystals, 2) solving structures of HIV and/or host proteins using high-throughput approaches for crystallization, data collection, and structure determination, and 3) carrying out SAXS analysis of proteins, with collaborative input from Dr. Yun-Xing Wang.
The PCHPI makes use of the X-ray facility of the Department of Structural Biology, which occupies ~1500 sq. ft. suite, on the first floor of BST3. The facility is partitioned into six rooms, containing multiple generators and detectors. The range of equipment available allows for optimal data collection from very small and normal sized crystals, and from crystals with large unit cells which typically contain very large proteins, viruses, or protein-protein assemblies. One of the generators also utilizes an ACTOR robot for automatically mounting and collecting data on a series of crystals, rapidly screening them for diffraction characteristics. Three additional labs, devoted to crystallization and computational analysis, contain equipment for automatic preparation of crystallization screening trays and for automatic and unattended imaging of these trays, as well as equipment for microscopy, and data analysis. The X-ray suite is supplemented by two environmentally controlled rooms dedicated to grow, store, and monitor crystals, at ambient temperature and at 4°C.