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.
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.
A microfocus macromolecular crystallography beamline at the Australian Synchrotron is presented.
Chromodomains are a superfamily of protein domains that are implicated in the modulation of chromatin structures. The chromodomain superfamily can be subdivided into two subfamilies, chromodomains ...and chromo shadow domains. Chromodomains function to localise proteins to specific sites on chromatin. An NMR structure of a chromodomain has been previously solved. Chromo shadow domains are protein-protein interaction domains. These recruit other chromatin associated proteins to their sites of action. The two domains have sequence similarities and are likely to have similar structures. The basis for their functional divergence is not known. In the present study, an X-ray structure of the chromo shadow domain of fission yeast Swi6 protein was solved to 1.9A. The structure reveals that the chromo shadow domain is a dimer with monomers closely resembling the chromodomain structure. Dimerisation of the chromo shadow domains creates a cleft that is commensurate with peptide binding. Binding studies were carried out to further investigate chromo shadow domain function. Recently, proteins of the Drosophila dosage compensation complex were found to contain divergent chromodomain-like regions. These domains have been noted to have RNA binding properties. Preliminary structural studies were carried out to determine if these domains shared a common fold with chromodomains and chromo shadow domains.
Chromodomains are a superfamily of protein domains that are implicated in the modulation of chromatin structures. The chromodomain superfamily can be subdivided into two subfamilies, chromodomains ...and chromo shadow domains. Chromodomains function to localise proteins to specific sites on chromatin. An NMR structure of a chromodomain has been previously solved. Chromo shadow domains are protein-protein interaction domains. These recruit other chromatin associated proteins to their sites of action. The two domains have sequence similarities and are likely to have similar structures. The basis for their functional divergence is not known. In the present study, an X-ray structure of the chromo shadow domain of fission yeast Swi6 protein was solved to 1.9A. The structure reveals that the chromo shadow domain is a dimer with monomers closely resembling the chromodomain structure. Dimerisation of the chromo shadow domains creates a cleft that is commensurate with peptide binding. Binding studies were carried out to further investigate chromo shadow domain function. Recently, proteins of the Drosophila dosage compensation complex were found to contain divergent chromodomain-like regions. These domains have been noted to have RNA binding properties. Preliminary structural studies were carried out to determine if these domains shared a common fold with chromodomains and chromo shadow domains.
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