Year: 2002
Type: conference-abstract
Abstract: A home laboratory high-intensity chromium X-ray source appears to be ideally suited for use in enhancing the weak anomalous signals from sulfur, selenium, calcium and other atoms found in protein crystals. Specifically, the f for sulfur is 1.14 at CrK which is similar to the f of calcium collected at CuK. Since calcium anomalous scattering has been used to phase trypsin [1] from CuK diffraction data, we expect a high quality CrK data set to provide even more phasing power and allow for routine phasing of macromolecular diffraction data without the need for synchrotron data or isomorphous replacement. In order to test this hypothesis we have commissioned Osmic, Inc. to design and manufacture a Confocal Max-Flux optic optimized specifically for Cr radiation. We are now performing experiments with this optic to determine how to maximize the anomalous signal from sulfur and other light elements within different proteins with the goal of solving the phase problem more readily. Special attention will be given to the details required to offset the strong absorption of Cr radiation by the experimental setup typically used for diffraction studies.
Institution: Rigaku (United States)
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2011315443