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Figure 1
Principle of biological SAXS measurements. (a) Schematic of a SAXS setup. At a synchrotron, electrons passing through an undulator (or wiggler or bending magnet) produce X-rays; alternatively an anode source is used at in-house setups. The beam is collimated and directed at a measurement cell filled with either protein sample or buffer only. A hybrid pixel detector records two-dimensional scattering images, which are transformed to one-dimensional scattering profiles. (b)–(c) One-dimensional scattering profiles from the sample (cytochrome c at 8 mg ml−1; dark blue) and buffer (light blue) and the resulting buffer-subtracted scattering profiles (green) obtained at (b) a synchrotron source (exposure time 1 s; BM29, ESRF, Grenoble) and (c) an in-house source (Bruetzel et al., 2016BB5) (exposure time 2 h; Department of Physics, LMU Munich).

Journal logoJOURNAL OF
APPLIED
CRYSTALLOGRAPHY
ISSN: 1600-5767
Volume 50| Part 2| April 2017| Pages 621-630
https://doi.org/10.1107/S1600576717003077
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