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	Super-resolution fluorescence imaging of cryosamples does not limit achievable resolution in cryoEM.
Journal, issue, pages	J Struct Biol, Vol. 215, Issue 4, Page 108040, Year 2023
Publish date	Oct 31, 2023
Authors	Mart G F Last / Willem E M Noteborn / Lenard M Voortman / Thomas H Sharp /
PubMed Abstract	Correlated super-resolution cryo-fluorescence and cryo-electron microscopy (cryoEM) has been gaining popularity as a method to investigate biological samples with high resolution and specificity. A ...Correlated super-resolution cryo-fluorescence and cryo-electron microscopy (cryoEM) has been gaining popularity as a method to investigate biological samples with high resolution and specificity. A concern in this combined method (called SR-cryoCLEM), however, is whether and how fluorescence imaging prior to cryoEM acquisition is detrimental to sample integrity. In this report, we investigated the effect of high-dose laser light (405, 488, and 561 nm) irradiation on apoferritin samples prepared for cryoEM with excitation wavelengths commonly used in fluorescence microscopy, and compared these samples to controls that were kept in the dark. We found that laser illumination, of equal duration and intensity as used in cryo-single molecule localization microscopy (cryoSMLM) and in the presence of high concentrations of fluorescent protein, did not affect the achievable resolution in cryoEM, with final reconstructions reaching resolutions of ∼ 1.8 Å regardless of the laser illumination. The finding that super-resolution fluorescence imaging of cryosamples prior to cryoEM data acquisition does not limit the achievable resolution suggests that super-resolution cryo-fluorescence microscopy and in situ structural biology using cryoEM are entirely compatible.
External links	J Struct Biol / PubMed:37918761
Methods	EM (single particle)
Resolution	1.76 - 1.82 Å
Structure data	16783 8cpm EMDB-16783, PDB-8cpm: Human apoferritin after 405 nm laser exposure Method: EM (single particle) / Resolution: 1.81 Å 16784 8cps EMDB-16784, PDB-8cps: Human apoferritin Method: EM (single particle) / Resolution: 1.82 Å 16785 8cpt EMDB-16785, PDB-8cpt: Human apoferritin after 488 nm laser exposure Method: EM (single particle) / Resolution: 1.79 Å 16786 8cpu EMDB-16786, PDB-8cpu: Human apoferritin after 561 nm laser exposure Method: EM (single particle) / Resolution: 1.76 Å 16787 8cpv EMDB-16787, PDB-8cpv: Human apoferritin Method: EM (single particle) / Resolution: 1.76 Å 16788 8cpw EMDB-16788, PDB-8cpw: Human apoferritin after 405 nm + 488 nm laser exposure in presence of rsEGFP2 Method: EM (single particle) / Resolution: 1.79 Å 16789 8cpx EMDB-16789, PDB-8cpx: Human apoferritin after 488 nm laser exposure in presence of rsEGFP2 Method: EM (single particle) / Resolution: 1.76 Å
Chemicals	ChemComp-NA: Unknown entry ChemComp-MG: Unknown entry ChemComp-HOH: WATER
Source	homo sapiens (human)
Keywords	METAL BINDING PROTEIN / Iron binding protein