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MX1: a bending-magnet crystallography beamline serving both chemical and macromolecular crystallography communities at the Australian Synchrotron - PubMed

MX1: a bending-magnet crystallography beamline serving both chemical and macromolecular crystallography communities at the Australian Synchrotron

Nathan Philip Cowieson et al. J Synchrotron Radiat. 2015 Jan.

Abstract

MX1 is a bending-magnet crystallography beamline at the 3 GeV Australian Synchrotron. The beamline delivers hard X-rays in the energy range from 8 to 18 keV to a focal spot at the sample position of 120 µm FWHM. The beamline endstation and ancillary equipment facilitate local and remote access for both chemical and biological macromolecular crystallography. Here, the design of the beamline and endstation are discussed. The beamline has enjoyed a full user program for the last seven years and scientific highlights from the user program are also presented.

Keywords: beamline; bending magnet; crystallography.

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Figures

Figure 1
Figure 1

Schematic layout of the MX1 beamline. Components are bending-magnet source (yellow), beam-defining masks (purple), safety shutters (peach), storage-ring wall (light grey), slits (blue), mirrors (white), monochromator (green), filter wheel (yellow), goniometer (dark grey) and CCD detector (pink). Distances are metres from the source.

Figure 2
Figure 2

(a) MX1 sample environment showing the fluorescence detector (FD), the rotation axis (RA), the cryojet (CJ) and illuminated back-stop (BS) projecting in from the bottom left, the sample light projecting in from the left middle (SL), and the UV laser for radiation-induced phasing (UV) projecting in from the top left. (b) Stick representation of a supramolecular assembly (Duriska et al., 2009a ,b ▶). The gold sphere is used to illustrate the void space and does not represent a real feature. (c) Orthogonal views of the B:C component complex (

4IGL

) of the bacterial ABC toxin. The C component is shown in red and the B component in grey. (d) View of a fragment bound to bovine trypsin (

4AB9

). Electron density around the fragment is show contoured at 1σ.

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