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. 2018 May 1;25(Pt 3):885-891.
doi: 10.1107/S1600577518003120. Epub 2018 Apr 3.

MX2: a high-flux undulator microfocus beamline serving both the chemical and macromolecular crystallography communities at the Australian Synchrotron

David Aragão  1 , Jun Aishima  1 , Hima Cherukuvada  1 , Robert Clarken  1 , Mark Clift  1 , Nathan Philip Cowieson  2 , Daniel Jesper Ericsson  1 , Christine L Gee  3 , Sofia Macedo  1 , Nathan Mudie  1 , Santosh Panjikar  1 , Jason Roy Price  1 , Alan Riboldi-Tunnicliffe  1 , Robert Rostan  1 , Rachel Williamson  1 , Thomas Tudor Caradoc-Davies  1
Affiliations

MX2: a high-flux undulator microfocus beamline serving both the chemical and macromolecular crystallography communities at the Australian Synchrotron

David Aragão et al. J Synchrotron Radiat. .

Abstract

MX2 is an in-vacuum undulator-based crystallography beamline at the 3 GeV Australian Synchrotron. The beamline delivers hard X-rays in the energy range 4.8-21 keV to a focal spot of 22 × 12 µm FWHM (H × V). At 13 keV the flux at the sample is 3.4 × 1012 photons s-1. The beamline endstation allows robotic handling of cryogenic samples via an updated SSRL SAM robot. This beamline is ideal for weakly diffracting hard-to-crystallize proteins, virus particles, protein assemblies and nucleic acids as well as smaller molecules such as inorganic catalysts and organic drug molecules. The beamline is now mature and has enjoyed a full user program for the last nine years. This paper describes the beamline status, plans for its future and some recent scientific highlights.

Keywords: EIGER detector; anomalous scattering; apertures; collimators; long wavelengths; macromolecular crystallography; microfocus beamlines; remote access; undulators.

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Figures

Figure 1
Figure 1
Schematic layout of the MX2 beamline. Components are undulator source (yellow), beam defining masks (purple), safety shutters (peach), slits (blue), mirrors (white), monochromator (green), goniometer (grey) and pixel array detector (pink). Distances are metres from the source.
Figure 2
Figure 2
MX2 sample environment showing the rotation axis (middle top); the cryostream and illuminated back-stop projecting in from middle bottom; the sample light projecting in from left to the sample and the EIGER X 16M detector on the right.
Figure 3
Figure 3
The beak and feather disease virus capsid built from 60 monomers of the capsid protein.
Figure 4
Figure 4
The space-filling structure of the interpenetrated porous metal organic framework (one network in red, the other in blue) showing the large void space.
See this image and copyright information in PMC

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Grants and funding

This work was funded by National eResearch Collaboration Tools and Resources (NeCTAR) project (NeCTAR, n.d.). grant . Australian Cancer Research Foundation (ACRF) grant .