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10.1016/j.abb.2016.03.036 http://scihub22266oqcxt.onion/10.1016/j.abb.2016.03.036 C4909539!4909539 !27143509     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27143509 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Arch+Biochem+Biophys 2016 ; 602 (ä): 32-47 Nephropedia Template TP {{tp|p=27143509 |t=2016. Serial femtosecond crystallography: A revolution in structural biology |pdf=|usr=}}{{27143509 }} gab.com Text Serial femtosecond crystallography: A revolution in structural biology JO: Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=27143509 #FOAvip Macromolecular crystallography at synchrotron sources has proven to be the most influential method within structural biology, producing thousands of structures since its inception. While its utility has been instrumental in progressing our knowledge of structures of molecules, it suffers from limitations such as the need for large, well-diffracting crystals, and radiation damage that can hamper native structural determination. The recent advent of X-ray free electron lasers (XFELs) and their implementation in the emerging field of serial femtosecond crystallography (SFX) has given rise to a remarkable expansion upon existing crystallographic constraints, allowing structural biologists access to previously restricted scientific territory. SFX relies on exceptionally brilliant, micro-focused X-ray pulses, which are femtoseconds in duration, to probe nano/micrometer sized crystals in a serial fashion. This results in data sets comprised of individual snapshots, each capturing Bragg diffraction of single crystals in random orientations prior to their subsequent destruction. Thus structural elucidation while avoiding radiation damage, even at room temperature, can now be achieved. This emerging field has cultivated new methods for nanocrystallogenesis, sample delivery, and data processing. Opportunities and challenges within SFX are reviewed herein. Twit Text FOAVip Serial femtosecond crystallography: A revolution in structural biology ????Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=27143509 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27143509 #FOAvip English Wikipedia <ref>{{Cite pmid|27143509 }}</ref> Serial femtosecond crystallography: A revolution in structural biology #MMPMID27143509 Martin-Garcia JM ; Conrad CE ; Coe J ; Roy-Chowdhury S ; Fromme P Arch Biochem Biophys 2016[Jul]; 602 (ä): 32-47 PMID27143509 show ga Macromolecular crystallography at synchrotron sources has proven to be the most influential method within structural biology, producing thousands of structures since its inception. While its utility has been instrumental in progressing our knowledge of structures of molecules, it suffers from limitations such as the need for large, well-diffracting crystals, and radiation damage that can hamper native structural determination. The recent advent of X-ray free electron lasers (XFELs) and their implementation in the emerging field of serial femtosecond crystallography (SFX) has given rise to a remarkable expansion upon existing crystallographic constraints, allowing structural biologists access to previously restricted scientific territory. SFX relies on exceptionally brilliant, micro-focused X-ray pulses, which are femtoseconds in duration, to probe nano/micrometer sized crystals in a serial fashion. This results in data sets comprised of individual snapshots, each capturing Bragg diffraction of single crystals in random orientations prior to their subsequent destruction. Thus structural elucidation while avoiding radiation damage, even at room temperature, can now be achieved. This emerging field has cultivated new methods for nanocrystallogenesis, sample delivery, and data processing. Opportunities and challenges within SFX are reviewed herein. |*Models, Molecular [MESH] |Computer Simulation [MESH] |Crystallization/*methods/trends [MESH] |Protein Conformation [MESH] |Proteins/*chemical synthesis/*ultrastructure [MESH]Serial femtosecond crystallography: A revolution in structural biology(epmc).pdf DeepDyve Pubget Overpricing