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10.1107/S205225251700570X http://scihub22266oqcxt.onion/10.1107/S205225251700570X C5571807!5571807 !28875031     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28875031 &cmd=llinks): Failed to open stream: HTTP request failed! 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Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation |pdf=|usr=}}{{28875031 }} gab.com Text Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation JO: IUCrJ http://www.kidney.de/pget.php?&tw=1&pmid=28875031 #FOAvip Crystal structure determination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render microfocus beamlines at synchrotron-radiation sources suitable for room-temperature serial crystallography data collection also. Owing to the longer exposure times that are needed at synchrotrons, serial data collection is termed serial millisecond crystallography (SMX). As a result, the number of SMX experiments is growing rapidly, with a dozen experiments reported so far. Here, the first high-viscosity injector-based SMX experiments carried out at a US synchrotron source, the Advanced Photon Source (APS), are reported. Microcrystals (5-20?µm) of a wide variety of proteins, including lysozyme, thaumatin, phycocyanin, the human A(2A) adenosine receptor (A(2A)AR), the soluble fragment of the membrane lipoprotein Flpp3 and proteinase K, were screened. Crystals suspended in lipidic cubic phase (LCP) or a high-molecular-weight poly(ethylene oxide) (PEO; molecular weight 8?000?000) were delivered to the beam using a high-viscosity injector. In-house data-reduction (hit-finding) software developed at APS as well as the SFX data-reduction and analysis software suites Cheetah and CrystFEL enabled efficient on-site SMX data monitoring, reduction and processing. Complete data sets were collected for A(2A)AR, phycocyanin, Flpp3, proteinase K and lysozyme, and the structures of A(2A)AR, phycocyanin, proteinase K and lysozyme were determined at 3.2, 3.1, 2.65 and 2.05?Å resolution, respectively. The data demonstrate the feasibility of serial millisecond crystallography from 5-20?µm crystals using a high-viscosity injector at APS. The resolution of the crystal structures obtained in this study was dictated by the current flux density and crystal size, but upcoming developments in beamline optics and the planned APS-U upgrade will increase the intensity by two orders of magnitude. These developments will enable structure determination from smaller and/or weakly diffracting microcrystals. Twit Text FOAVip Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation ????IUCrJ http://www.kidney.de/pget.php?&tw=1&pmid=28875031 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28875031 #FOAvip English Wikipedia <ref>{{Cite pmid|28875031 }}</ref> Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation #MMPMID28875031 Martin-Garcia JM ; Conrad CE ; Nelson G ; Stander N ; Zatsepin NA ; Zook J ; Zhu L ; Geiger J ; Chun E ; Kissick D ; Hilgart MC ; Ogata C ; Ishchenko A ; Nagaratnam N ; Roy-Chowdhury S ; Coe J ; Subramanian G ; Schaffer A ; James D ; Ketwala G ; Venugopalan N ; Xu S ; Corcoran S ; Ferguson D ; Weierstall U ; Spence JCH ; Cherezov V ; Fromme P ; Fischetti RF ; Liu W IUCrJ 2017[Jul]; 4 (Pt 4 ): 439-454 PMID28875031 show ga Crystal structure determination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render microfocus beamlines at synchrotron-radiation sources suitable for room-temperature serial crystallography data collection also. Owing to the longer exposure times that are needed at synchrotrons, serial data collection is termed serial millisecond crystallography (SMX). As a result, the number of SMX experiments is growing rapidly, with a dozen experiments reported so far. Here, the first high-viscosity injector-based SMX experiments carried out at a US synchrotron source, the Advanced Photon Source (APS), are reported. Microcrystals (5-20?µm) of a wide variety of proteins, including lysozyme, thaumatin, phycocyanin, the human A(2A) adenosine receptor (A(2A)AR), the soluble fragment of the membrane lipoprotein Flpp3 and proteinase K, were screened. Crystals suspended in lipidic cubic phase (LCP) or a high-molecular-weight poly(ethylene oxide) (PEO; molecular weight 8?000?000) were delivered to the beam using a high-viscosity injector. In-house data-reduction (hit-finding) software developed at APS as well as the SFX data-reduction and analysis software suites Cheetah and CrystFEL enabled efficient on-site SMX data monitoring, reduction and processing. Complete data sets were collected for A(2A)AR, phycocyanin, Flpp3, proteinase K and lysozyme, and the structures of A(2A)AR, phycocyanin, proteinase K and lysozyme were determined at 3.2, 3.1, 2.65 and 2.05?Å resolution, respectively. The data demonstrate the feasibility of serial millisecond crystallography from 5-20?µm crystals using a high-viscosity injector at APS. The resolution of the crystal structures obtained in this study was dictated by the current flux density and crystal size, but upcoming developments in beamline optics and the planned APS-U upgrade will increase the intensity by two orders of magnitude. These developments will enable structure determination from smaller and/or weakly diffracting microcrystals. äSerial millisecond crystallography of membrane and soluble protein mic(epmc).pdf DeepDyve Pubget Overpricing