Microcrystallography using single-bounce monocapillary optics.
X-ray microbeams have become increasingly valuable in protein crystallography. A number of synchrotron beamlines worldwide have adapted to handling smaller and more challenging samples by providing a combination of high-precision sample-positioning hardware, special visible-light optics for sample visualization, and small-diameter X-ray beams with low background scatter. Most commonly, X-ray microbeams with diameters ranging from 50 microm to 1 microm are produced by Kirkpatrick and Baez mirrors in combination with defining apertures and scatter guards. A simple alternative based on single-bounce glass monocapillary X-ray optics is presented. The basic capillary design considerations are discussed and a practical and robust implementation that capitalizes on existing beamline hardware is presented. A design for mounting the capillary is presented which eliminates parasitic scattering and reduces deformations of the optic to a degree suitable for use on next-generation X-ray sources. Comparison of diffraction data statistics for microcrystals using microbeam and conventional aperture-collimated beam shows that capillary-focused beam can deliver significant improvement. Statistics also confirm that the annular beam profile produced by the capillary optic does not impact data quality in an observable way. Examples are given of new structures recently solved using this technology. Single-bounce monocapillary optics can offer an attractive alternative for retrofitting existing beamlines for microcrystallography.
MacCHESS (Macromolecular Diffraction Facility at CHESS), Ithaca, NY, USA. reg8@cornell.edu
R E
RE
Gillilan
M J
MJ
Cook
S W
SW
Cornaby
D H
DH
Bilderback
D018360:Crystallography, X-Ray / Q000379:methods*; D019286:Endopeptidase K / Q000737:chemistry; D055095:Optics and Photonics / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation
D011506:Proteins; D019286:Endopeptidase K