About the Core
Single crystal X-ray diffraction remains the most powerful technique to determine the three-dimensional structure of biologically important macromolecules and their functional ligand complexes at or near atomic resolution. The purpose of the Macromolecular X-ray Crystallography ATC is to provide a cost-efficient solution for scientists, researchers, and trainees at Baylor College of Medicine and the Texas Medical Center to pursue high-resolution structural studies. X-ray crystallography is not limited by the size or nature of the specimen, making it possible to determine the three-dimensional structure of nucleic acids and other small macromolecules to multi-subunit macromolecular assemblies.
X-ray Crystallography Advantages
One of the major advantages of X-ray crystallography is that atomic or near atomic resolution structural information can be obtained routinely, thereby revealing intimate details regarding the stereo-chemistry of the molecular interactions underlying the biological function of the macromolecule of interest. Finally, X-ray crystallography allows the three-dimensional structure determination of a macromolecule bound to an agonist or antagonist with little additional effort. The structure of such a complex is highly valuable, and the molecular insight thus obtained is frequently exploited for rationale structure-based drug design.
A new Formulatrix Rock Imager 2 capable of UV and Multi-fluorescence Imaging was acquired through an NIH Shared Instrumentation Grant Award (S10OD030246, Protein Crystallization Imager) and installed in 2022. Please remember to acknowledge our funding source in publications that use data produced by our core.
The BCM Macromolecular X-ray crystallography core is supported in part by an NIH Shared Instrumentation Grant Award (S10OD030246, Protein Crystallization Imager)
