The instrument is a high intensity bending magnet beam line utilising 4:1 demagnifying optics in both the horizontal and vertical directions. The beam is first monochromatised and focused in the horizontal by a single Ge(111) triangular bent crystal. Afte rwards the beam is incident on a vertically focusing mirror consisting of 12 flat quartz segments mounted on a common bender. The beam enters the experimental hutch through a Be window and can then be collimated using two pairs of slits before it reaches the sample. The collimator, rotation camera, detector and cryogenic cooling unit are all mounted on a common optical bench which can be automatically adjusted to maximise the X-ray flux on the sample.
Although the X-ray wavelength may be tuned by rotating the mirror and the optical bench around the monochromator position together with a simultaneous change in the monochromator Bragg angle the beam line is typically operated at a fixed wavelength of 0.9 3 Å.
All optical elements are controlled through CAMAC modules by a PC. Data collection is controlled from an SGI Indy workstation.
Protein crystallography.
J. Hendrix, M.H.J. Koch and J. Bordas., J. Appl. Cryst. 12 (1979) 467-472
|
Source (4.5 GeV) |
bending magnet Ec = 16.6 keV |
|---|---|
|
Monochromator |
Ge(111) triangular bent |
|
Mirror |
elliptically bent 12 quartz segments |
|
Demagnification |
4:1 |
|
Beam size at sample |
~ 0.5 x 1.5 mm2 FWHM |
|
Wavelength |
0.93 Å |
|
Wavelength bandpass |
2 x 10-3 (Δλ/λ) |
|
Detector |
MAR imaging plate scanner (300 nm plate) |
|
Cryogenic cooling |
Oxford Instruments cryo unit; Tmin = 90 K |
|
Sample-detector |
85 mm - 700 mm |