New Approach for Solving Protein Structures from Tiny Crystals
Using X-rays to reveal the atomic-scale three-dimensional structures of proteins has led to countless advances in understanding how these molecules function in bacteria, viruses, plants, and humans. To grow some proteins into crystals large enough for this approach, scientists at the U.S. Department of Energy’s (DOE) Brookhaven National Laboratory (BNL) and colleagues at Columbia University developed an approach for solving protein structures from tiny crystals. To examine previously inaccessible microcrystals, they are using unique sample-handling, signal-extraction, and data-assembly approaches, along with a beamline capable of focusing intense X-rays at Brookhaven National Laboratory’s National Synchrotron Light Source II.
Guo, G., et al. “Sample Manipulation and Data Assembly for Robust Microcrystal Synchrotron Crystallography.” IUCrJ 5(Part 3) 238–46 (2018). [DOI: https://doi.org/10.1107/S2052252518005389]