Presented by Dr. Paul Adams, senior scientist, Physical Biosciences Division, Lawrence Berkeley Laboratory & professor, Department of Bioengineering, University of California Berkeley.

X-ray crystallography is a well-established technique that is now routinely used to determine the structures of macromolecules. It is able to provide atomic resolution information that has been a prerequisite to the understanding the fundamentals of life, from the structure of the double helix to the structures of intact ribosomes. It is also a method that is central to the development of new therapeutics for human disease. Increasingly, researchers are studying larger complexes and/or systems will inherent flexibility, often leading to low resolution diffraction data. This lack of experimental observations presents challenges for obtaining high quality atomic models. Therefore, we have developed a low-resolution crystallographic refinement method that combines the Rosetta sampling methodology and energy function with reciprocal-space X-ray refinement in Phenix. On a set of difficult low-resolution refinement cases, we see improved model geometry and lower free R-factors compared to alternate refinement methods.

All Biochemistry/Redox Biology Center Seminars are free and open to the public.