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10.1016/j.str.2020.11.001 http://scihub22266oqcxt.onion/10.1016/j.str.2020.11.001 C7867593!7867593!33217329     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Structure 2021 ; 29 (2): 186-195.e6 Nephropedia Template TP {{tp|p=33217329|t=2021. Native mass spectrometry-based screening for optimal sample preparation in single particle cryo-EM |pdf=|usr=}}{{33217329}} gab.com Text Native mass spectrometry-based screening for optimal sample preparation in single particle cryo-EM JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=33217329 #FOAvip Recent advances in single particle cryogenic electron microscopy (cryo-EM) have enabled the structural determination of numerous protein assemblies at high resolution, yielding unprecedented insights into their function. However, despite its extraordinary capabilities, cryo-EM remains time-consuming and resource-intensive. It is therefore beneficial to have a means for rapidly assessing and optimizing the quality of samples prior to lengthy cryo-EM analyses. To do this, we have developed a native mass spectrometry (nMS) platform that provides rapid feedback on sample quality and highly streamlined biochemical screening. Because nMS enables accurate mass analysis of protein complexes, it is well-suited for routine evaluation of the composition, integrity, and homogeneity of samples prior to their plunge-freezing on EM grids. We demonstrate the utility of our nMS-based platform for facilitating cryo-EM studies using structural characterizations of exemplar bacterial transcription complexes as well as the replication-transcription assembly from the SARS-CoV-2 virus that is responsible for the COVID-19 pandemic. Twit Text FOAVip Native mass spectrometry-based screening for optimal sample preparation in single particle cryo-EM ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=33217329 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33217329 #FOAvip English Wikipedia <ref>{{Cite pmid|33217329}}</ref> Native mass spectrometry-based screening for optimal sample preparation in single particle cryo-EM #MMPMID33217329 Olinares PDB; Kang JY; Llewellyn E; Chiu C; Chen J; Malone B; Saecker RM; Campbell EA; Darst SA; Chait BT Structure 2021[Feb]; 29 (2): 186-195.e6 PMID33217329show ga Recent advances in single particle cryogenic electron microscopy (cryo-EM) have enabled the structural determination of numerous protein assemblies at high resolution, yielding unprecedented insights into their function. However, despite its extraordinary capabilities, cryo-EM remains time-consuming and resource-intensive. It is therefore beneficial to have a means for rapidly assessing and optimizing the quality of samples prior to lengthy cryo-EM analyses. To do this, we have developed a native mass spectrometry (nMS) platform that provides rapid feedback on sample quality and highly streamlined biochemical screening. Because nMS enables accurate mass analysis of protein complexes, it is well-suited for routine evaluation of the composition, integrity, and homogeneity of samples prior to their plunge-freezing on EM grids. We demonstrate the utility of our nMS-based platform for facilitating cryo-EM studies using structural characterizations of exemplar bacterial transcription complexes as well as the replication-transcription assembly from the SARS-CoV-2 virus that is responsible for the COVID-19 pandemic. äNative mass spectrometry-based screening for optimal sample preparatio(epmc).pdf DeepDyve Pubget Overpricing