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Beamline: K1.3 (EMBL X11)

Protein Crystallography (EMBL X11)

K1.3

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.

Applications

Protein crystallography.

Literature on Instrumentation

J. Hendrix, M.H.J. Koch and J. Bordas., J. Appl. Cryst. 12 (1979) 467-472

Instrument Specification

Source (4.5 GeV)

bending magnet Ec = 16.6 keV
beam size 1.3 x 4.4 mm2 FWHM
vert. electron beam divergence 0.06 mrad FWHM

Monochromator

Ge(111) triangular bent
compressing 7° Fankuchen cut

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


 
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