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10.1107/S2059798317004077 http://scihub22266oqcxt.onion/10.1107/S2059798317004077 C5458495!5458495 !28580915     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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 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\28580915 .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+Struct+Biol 2017 ; 73 (Pt 6 ): 534-540 Nephropedia Template TP {{tp|p=28580915 |t=2017. The potential use of single-particle electron microscopy as a tool for structure-based inhibitor design |pdf=|usr=}}{{28580915 }} gab.com Text The potential use of single-particle electron microscopy as a tool for structure-based inhibitor design JO: Acta Crystallogr D Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=28580915 #FOAvip Recent developments in electron microscopy (EM) have led to a step change in our ability to solve the structures of previously intractable systems, especially membrane proteins and large protein complexes. This has provided new opportunities in the field of structure-based drug design, with a number of high-profile publications resolving the binding sites of small molecules and peptide inhibitors. There are a number of advantages of EM over the more traditional X-ray crystallographic approach, such as resolving different conformational states and permitting the dynamics of a system to be better resolved when not constrained by a crystal lattice. There are still significant challenges to be overcome using an EM approach, not least the speed of structure determination, difficulties with low-occupancy ligands and the modest resolution that is available. However, with the anticipated developments in the field of EM, the potential of EM to become a key tool for structure-based drug design, often complementing X-ray and NMR studies, seems promising. Twit Text FOAVip The potential use of single-particle electron microscopy as a tool for structure-based inhibitor design ????Acta Crystallogr D Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=28580915 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28580915 #FOAvip English Wikipedia <ref>{{Cite pmid|28580915 }}</ref> The potential use of single-particle electron microscopy as a tool for structure-based inhibitor design #MMPMID28580915 Rawson S ; McPhillie MJ ; Johnson RM ; Fishwick CWG ; Muench SP Acta Crystallogr D Struct Biol 2017[Jun]; 73 (Pt 6 ): 534-540 PMID28580915 show ga Recent developments in electron microscopy (EM) have led to a step change in our ability to solve the structures of previously intractable systems, especially membrane proteins and large protein complexes. This has provided new opportunities in the field of structure-based drug design, with a number of high-profile publications resolving the binding sites of small molecules and peptide inhibitors. There are a number of advantages of EM over the more traditional X-ray crystallographic approach, such as resolving different conformational states and permitting the dynamics of a system to be better resolved when not constrained by a crystal lattice. There are still significant challenges to be overcome using an EM approach, not least the speed of structure determination, difficulties with low-occupancy ligands and the modest resolution that is available. However, with the anticipated developments in the field of EM, the potential of EM to become a key tool for structure-based drug design, often complementing X-ray and NMR studies, seems promising. |*Drug Design [MESH] |Animals [MESH] |Ligands [MESH] |Microscopy, Electron/*methods [MESH] |Models, Molecular [MESH] |Plasmodium falciparum/enzymology/ultrastructure [MESH] |Proteasome Endopeptidase Complex/metabolism/ultrastructure [MESH] |Rats [MESH] |Saccharomyces cerevisiae Proteins/metabolism/ultrastructure [MESH] |Saccharomyces cerevisiae/metabolism/ultrastructure [MESH]The potential use of single-particle electron microscopy as a tool for(epmc).pdf DeepDyve Pubget Overpricing