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10.1016/j.sbi.2014.07.005 http://scihub22266oqcxt.onion/10.1016/j.sbi.2014.07.005 C4253534!4253534!25113271     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Opin+Struct+Biol 2014 ; ä (ä): 56-62 Nephropedia Template TP {{tp|p=25113271|t=2014. E pluribus unum, no more: From one crystal, many conformations |pdf=|usr=}}{{25113271}} gab.com Text E pluribus unum, no more: From one crystal, many conformations JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=25113271 #FOAvip Several distinct computational approaches have recently been implemented to represent conformational heterogeneity from time- and space-averaged X-ray crystallography datasets. As these modeling methods mature, newly discovered alternative conformations are being used to derive functional protein mechanisms. Room temperature X-ray data collection is emerging as a key variable for sampling functionally relevant conformations also observed in solution studies. Although concerns about radiation damage are warranted with higher temperature data collection, ?diffract and destroy? strategies on X-ray free electron lasers may permit radiation damage-free data collection. X-ray crystallography need not be confined to ?static unique snapshots?; these experimental and computational advances are revealing how the many conformations populated within a single crystal are used in biological mechanisms. Twit Text FOAVip E pluribus unum, no more: From one crystal, many conformations ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=25113271 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25113271 #FOAvip English Wikipedia <ref>{{Cite pmid|25113271}}</ref> E pluribus unum, no more: From one crystal, many conformations #MMPMID25113271 Woldeyes RA; Sivak DA; Fraser JS Curr Opin Struct Biol 2014[Oct]; ä (ä): 56-62 PMID25113271show ga Several distinct computational approaches have recently been implemented to represent conformational heterogeneity from time- and space-averaged X-ray crystallography datasets. As these modeling methods mature, newly discovered alternative conformations are being used to derive functional protein mechanisms. Room temperature X-ray data collection is emerging as a key variable for sampling functionally relevant conformations also observed in solution studies. Although concerns about radiation damage are warranted with higher temperature data collection, ?diffract and destroy? strategies on X-ray free electron lasers may permit radiation damage-free data collection. X-ray crystallography need not be confined to ?static unique snapshots?; these experimental and computational advances are revealing how the many conformations populated within a single crystal are used in biological mechanisms. äE pluribus unum, no more: From one crystal, many conformations (epmc).pdf DeepDyve Pubget Overpricing