Protein crystallography using a multilayer monochromator

Abstract

A multilayer monochromator was installed on a bending-magnet beamline at the Cornell High Energy Synchrotron Source (CHESS) and was used to provide an unfocused pseudo-monochromatic X-ray beam for protein crystallography experiments. Datasets were collected from lysozyme at room temperature and human methylthioadenosine phosphorylase at 100 K. The wide energy bandpass of the multilayer allowed short exposure times, typically only a few times longer than on a focused multipole wiggler beamline. The diffraction images were processed using unmodified monochromatic data-processing software to yield datasets of good quality. These first measurements demonstrate that multilayer monochromators can be readily applied to the rapid structure determination of many typical-sized macromolecules.