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An optimized collimator for X‐ray diffraction from very small samples using synchrotron radiation
Author(s) -
Bartunik H. D.,
Gehrmann T.,
Robrahn B.
Publication year - 1984
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889884011109
Subject(s) - collimator , synchrotron radiation , x ray , optics , diffraction , synchrotron , materials science , x ray crystallography , radiation , physics , crystallography , chemistry
The high intensity available from synchrotron radiation sources like DORIS allows one to reduce substantially the sample size required for biologicalstructure determination by X-ray techniques. One particular example is the possibil i~ (Bartunik, Fourme & Phillips, 1982) of collecting on a double-focusing X-ray camera, like the X l l at DORIS, highresolution data for three-dimensional protein-structure analysis from crystals as small as 10-20 t~m. Such applications require a collimator system which provides an optimum signal-to-noise ratio, and which may be aligned with high accuracy, possibly under remote control using the synchrotron-radiation beam. Such an optimized collimator has been developed and is described in the following. Two of these collimators are in routine use in diffraction studies of twoand three-dimensionally ordered biological structures on a modified Arndt-Wonacott rotation camera on the X l l and on a fourcircle diffractometer on the X31 at DORIS (Bartunik & Bartels, 1984). Fig. 1 shows the collimator system mounted on the rotation camera. The collimator incorporates two x-ytantalum slits (purchased from Huber, Rimsting) which serve as defining (DS) and guard slits (GS), respectively. DS defines the