Expanding the femtosecond crystallography toolkit
Year: 2014
Type: article
Abstract: The “21st century of biology” is built on advances in protein structure determination developed over the last five decades. Exponential growth in the number of determined protein structures has largely been driven by new technologies in protein X-ray crystallography, including synchrotron X-ray sources, X-ray detectors, computational tools, and methods of handling protein crystals. In consequence, the time to acquire a routine, complete crystallographic dataset has gone from years to minutes. However, many important macromolecular structures are still undetermined and many challenges remain, especially in cases where crystals are either hard to obtain, particularly sensitive to X-ray damage, or exhibit transient states that are difficult to capture by structural analysis. The latest tool in the crystallographic arsenal, the X-ray free electron laser (XFEL) (1), promises to help surmount these challenges (2), provided efficient ways are found to handle crystals in the demanding XFEL environment. In PNAS, Cohen et al. (3) show that crystal handling technology developed primarily for use at synchrotron storage ring X-ray sources can also be effectively adapted for use at XFELs.
Author: Sol M. Gruner
Institutions: Cornell University, Cornell High Energy Synchrotron Source
Language: English
Subfield: Radiation
Field: Physics and Astronomy
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W1497189187