Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Need for Speed: Examining Protein Behavior during CryoEM Grid Preparation at Different Timescales.
Journal, issue, pages	Structure, Vol. 28, Issue 11, Page 1238-11248.e4, Year 2020
Publish date	Nov 3, 2020
Authors	David P Klebl / Molly S C Gravett / Dimitrios Kontziampasis / David J Wright / Robin S Bon / Diana C F Monteiro / Martin Trebbin / Frank Sobott / Howard D White / Michele C Darrow / Rebecca F Thompson / Stephen P Muench /
PubMed Abstract	A host of new technologies are under development to improve the quality and reproducibility of cryoelectron microscopy (cryoEM) grid preparation. Here we have systematically investigated the ...A host of new technologies are under development to improve the quality and reproducibility of cryoelectron microscopy (cryoEM) grid preparation. Here we have systematically investigated the preparation of three macromolecular complexes using three different vitrification devices (Vitrobot, chameleon, and a time-resolved cryoEM device) on various timescales, including grids made within 6 ms (the fastest reported to date), to interrogate particle behavior at the air-water interface for different timepoints. Results demonstrate that different macromolecular complexes can respond to the thin-film environment formed during cryoEM sample preparation in highly variable ways, shedding light on why cryoEM sample preparation can be difficult to optimize. We demonstrate that reducing time between sample application and vitrification is just one tool to improve cryoEM grid quality, but that it is unlikely to be a generic "silver bullet" for improving the quality of every cryoEM sample preparation.
External links	Structure / PubMed:32814033 / PubMed Central
Methods	EM (single particle)
Resolution	4.1 - 9.4 Å
Structure data	EMDB-10871: 30S ribosome subunit deposited by spraying (13 ms delay) Method: EM (single particle) / Resolution: 9.4 Å EMDB-10872: 30S ribosome subunit deposited using the chameleon (54 ms delay) Method: EM (single particle) / Resolution: 7.1 Å EMDB-10873: 30S ribosome subunit deposited using the chameleon (200 ms delay) Method: EM (single particle) / Resolution: 6.8 Å EMDB-10874: 30S ribosome subunit prepared by blotting Method: EM (single particle) / Resolution: 6.8 Å EMDB-10875: 50S ribosome subunit deposited by spraying (13 ms delay) Method: EM (single particle) / Resolution: 5.1 Å EMDB-10876: 50S ribosome subunit deposited using the chameleon (54 ms delay) Method: EM (single particle) / Resolution: 4.5 Å EMDB-10877: 50S ribosome subunit deposited using the chameleon (200 ms delay) Method: EM (single particle) / Resolution: 4.1 Å EMDB-10878: 50S ribosome subunit prepared by blotting Method: EM (single particle) / Resolution: 4.4 Å EMDB-10879: 70S ribosome deposited by spraying (13 ms delay) Method: EM (single particle) / Resolution: 8.9 Å EMDB-10880: 70S ribosome deposited using the chameleon (54 ms delay) Method: EM (single particle) / Resolution: 5.8 Å EMDB-10881: 70S ribosome deposited using the chameleon (200 ms delay) Method: EM (single particle) / Resolution: 4.9 Å EMDB-10882: 70S ribosome prepared by blotting Method: EM (single particle) / Resolution: 5.1 Å EMDB-10883: HSPD1 single ring deposited by spraying (6 ms delay) Method: EM (single particle) / Resolution: 7.0 Å EMDB-10884: HSPD1 single ring deposited by spraying (50 ms delay) Method: EM (single particle) / Resolution: 6.8 Å EMDB-10885: HSPD1 single ring deposited using the chameleon (54 ms delay) Method: EM (single particle) / Resolution: 8.0 Å EMDB-10886: HSPD1 single ring prepared by blotting Method: EM (single particle) / Resolution: 7.1 Å
Source	Escherichia coli (E. coli) Homo sapiens (human)