RESUMO
A new high-pressure single-crystal diffraction setup has been designed and implemented at the Australian Synchrotron for collecting molecular and protein crystal structures. The setup incorporates a modified micro-Merrill-Bassett cell and holder designed specifically to fit onto the horizontal air-bearing goniometer, allowing high-pressure diffraction measurements to be collected with little to no modification of the beamline setup compared with ambient data collections. Compression data for the amino acid, L-threonine, and the protein, hen egg-white lysozyme, were collected, showcasing the capabilities of the setup.
Assuntos
Proteínas , Síncrotrons , Austrália , Cristalografia por Raios X , Proteínas/química , AminoácidosRESUMO
MX2 is an in-vacuum undulator-based crystallography beamline at the 3â GeV Australian Synchrotron. The beamline delivers hard X-rays in the energy range 4.8-21â keV to a focal spot of 22 × 12â µm FWHM (H × V). At 13â keV the flux at the sample is 3.4 × 1012â 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.