Polycapillary optic–source combinations for protein crystallography

Abstract

The work in this paper is a systematic study of the application of collimating and slightly focusing polycapillary optics to the X-ray crystallographic structure determination of egg-white lysozyme using two different sources: a standard rotating anode source and a low-power table-top microfocusing source. For the rotating anode source, a series of measurements comparing duplicate data sets obtained from the same individual crystal are summarized. Intensity and data quality are discussed for measurements with a pinhole collimator, a collimating polycapillary optic and a focusing polycapillary optic. The collected data were analyzed using conventional analysis software; limitations of the use of conventional analysis software for focused beams are discussed. Two data sets were collected using the low-power source and collimating optics, and three data sets using a lower-power source and focusing optics with three different limiting apertures.