Summary Large single crystals (up to 1 mm in each dimension) of the B800–850 antenna complex from Rhodopseudomonas acidophila strain 10050 have been grown in the presence of β-octyl-glucoside. These crystals have the space group R32 and unit cell dimensions of a = b = 119.9 Å and c = 297.0 Å. Recently we have improved our crystallization procedures so that all crystals now diffract reliably to beyond 3.5 Å, with some diffracting to below 3 Å. A range of isomorphous heavy atom derivatives have been prepared and we are now engaged in locating the heavy atom sites within the unit cell.
MAX IV is the first 'fourth-generation' synchrotron in the world [1] and it will start to produce the brightest light from this summer and onwards.As the first MX beamline at MAX IV, BioMAX will not only have highly brilliant X-ray beam but also high performance hardware [2,3], including the next generation hybrid pixel-array detector EIGER 16M, a newly developed fast sample changer ISARA and a high precision MD3 diffractometer.To take full advantage of these cutting edge technologies and to provide a more user friendly software interface particularly for the arising remote access, a new web-based version of a beamline and experiment control software MXCuBE3 has been being developed by MAX IV in strong collaboration with the ESRF.The software will support both single sample and in situ plate manipulation with modern acquisition methods, such as mesh scan and raster scan.Users can carry out their experiments through web browsers from any place and any operating system, without installation of any additional software.Following these high throughput experiments, a fast and accurate data processing pipeline becomes critical to meet the high data rate.While testing and comparing various existing processing pipelines that utilize XDS and Dials, we are also seeking new approaches that can handle the diffraction images.Finally, the experimental meta-data and processing results will be stored in our ISPyB server and users can access them via web browsers.
Antibodies to citrulline-modified proteins have a high diagnostic value in rheumatoid arthritis (RA). However, their biological role in disease development is still unclear. To obtain insight into this question, a panel of mouse monoclonal antibodies was generated against a major triple helical collagen type II (CII) epitope (position 359–369; ARGLTGRPGDA) with or without arginines modified by citrullination. These antibodies bind cartilage and synovial tissue, and mediate arthritis in mice. Detection of citrullinated CII from RA patients' synovial fluid demonstrates that cartilage-derived CII is indeed citrullinated in vivo. The structure determination of a Fab fragment of one of these antibodies in complex with a citrullinated peptide showed a surprising β-turn conformation of the peptide and provided information on citrulline recognition. Based on these findings, we propose that autoimmunity to CII, leading to the production of antibodies specific for both native and citrullinated CII, is an important pathogenic factor in the development of RA.
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