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10.1107/S0907444913003454 http://scihub22266oqcxt.onion/10.1107/S0907444913003454 C3663119!3663119 !23695239     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\23695239 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Acta+Crystallogr+D+Biol+Crystallogr 2013 ; 69 (Pt 6 ): 946-59 Nephropedia Template TP {{tp|p=23695239 |t=2013. Resolution of structural heterogeneity in dynamic crystallography |pdf=|usr=}}{{23695239 }} gab.com Text Resolution of structural heterogeneity in dynamic crystallography JO: Acta Crystallogr D Biol Crystallogr http://www.kidney.de/pget.php?&tw=1&pmid=23695239 #FOAvip Dynamic behavior of proteins is critical to their function. X-ray crystallography, a powerful yet mostly static technique, faces inherent challenges in acquiring dynamic information despite decades of effort. Dynamic `structural changes' are often indirectly inferred from `structural differences' by comparing related static structures. In contrast, the direct observation of dynamic structural changes requires the initiation of a biochemical reaction or process in a crystal. Both the direct and the indirect approaches share a common challenge in analysis: how to interpret the structural heterogeneity intrinsic to all dynamic processes. This paper presents a real-space approach to this challenge, in which a suite of analytical methods and tools to identify and refine the mixed structural species present in multiple crystallographic data sets have been developed. These methods have been applied to representative scenarios in dynamic crystallography, and reveal structural information that is otherwise difficult to interpret or inaccessible using conventional methods. Twit Text FOAVip Resolution of structural heterogeneity in dynamic crystallography ????Acta Crystallogr D Biol Crystallogr http://www.kidney.de/pget.php?&tw=1&pmid=23695239 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23695239 #FOAvip English Wikipedia <ref>{{Cite pmid|23695239 }}</ref> Resolution of structural heterogeneity in dynamic crystallography #MMPMID23695239 Ren Z ; Chan PW ; Moffat K ; Pai EF ; Royer WE Jr ; ?rajer V ; Yang X Acta Crystallogr D Biol Crystallogr 2013[Jun]; 69 (Pt 6 ): 946-59 PMID23695239 show ga Dynamic behavior of proteins is critical to their function. X-ray crystallography, a powerful yet mostly static technique, faces inherent challenges in acquiring dynamic information despite decades of effort. Dynamic `structural changes' are often indirectly inferred from `structural differences' by comparing related static structures. In contrast, the direct observation of dynamic structural changes requires the initiation of a biochemical reaction or process in a crystal. Both the direct and the indirect approaches share a common challenge in analysis: how to interpret the structural heterogeneity intrinsic to all dynamic processes. This paper presents a real-space approach to this challenge, in which a suite of analytical methods and tools to identify and refine the mixed structural species present in multiple crystallographic data sets have been developed. These methods have been applied to representative scenarios in dynamic crystallography, and reveal structural information that is otherwise difficult to interpret or inaccessible using conventional methods. |Algorithms [MESH] |Computational Biology/*methods [MESH] |Computer Simulation [MESH] |Crystallography/*methods [MESH] |Hemoglobins/chemistry [MESH] |Hydrolases/chemistry [MESH] |Macromolecular Substances/*chemistry [MESH]Resolution of structural heterogeneity in dynamic crystallography (epmc).pdf DeepDyve Pubget Overpricing