Comparison of the FR-E and RU-H2R X-ray sources for protein crystallography applications

Karl A. Byriel^a, Anna Aagaard^a, Christine L. Gee^a, Nirajali Gamage^b and Jennifer L. Martin^a

^aInstitute for Molecular Bioscience, The University of Queensland, QLD 4072 Australia; ^bDepartment of Physiology and Pharmacology, The University of Queensland, QLD 4072 Australia (k.byriel@imb.uq.edu.au)

The FR-E Superbright rotating anode generator was designed as a successor to the FR-D generator. It provides a high brilliance focal spot, 2.0 kW at 0.07 x 0.07 mm compared to the traditional home source RU-H2R or RU-H3R focal spot 5.0 kW at 0.3 x 3 mm or the FR-D focal spot 3.5 kW at 0.1 x 0.1 mm or 5.0 kW at 0.15 x 0.15 mm. The FR-E has the advantage of lower maintenance and easier handling than the FR-D.

Preliminary data will be presented for the comparison of the RU-H2R rotating anode generator and MSC Confocal Blue-3 optic against the FR-E Superbright generator with both MSC Confocal HiRes² and MaxScreen optics. Data in both cases are measured on an R-AXIS IV++ detector and the cryocooling apparatus is the same in each case, the CryoIndustries Cryocool NFC 1259 XRD.

We will present the results of characterization of the physical properties of the X-ray beam and data sets collected on the same small frozen lysozyme crystal from these systems. Results will also be presented for other protein crystal samples as they become available.