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	MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony.
Journal, issue, pages	Nat Methods, Vol. 22, Issue 12, Page 2563-2573, Year 2025
Publish date	Nov 13, 2025
Authors	Gangadhar Eluru / Steven De Gieter / Stephan Schenck / Annelore Stroobants / Binesh Shrestha / Paul Erbel / Janine D Brunner / Rouslan G Efremov /
PubMed Abstract	Single-particle cryogenic electron microscopy (cryo-EM) enables reconstruction of atomic-resolution 3D maps of proteins by visualizing thousands to millions of purified protein particles embedded in ...Single-particle cryogenic electron microscopy (cryo-EM) enables reconstruction of atomic-resolution 3D maps of proteins by visualizing thousands to millions of purified protein particles embedded in vitreous ice. This corresponds to picograms of purified protein, which can potentially be isolated from a few thousand cells. Hence, cryo-EM holds the potential of a very sensitive analytical method for delivering high-resolution protein structure as a readout. In practice, millions of times more starting biological material is required to prepare cryo-EM grids. Here we show that using a micro isolation (MISO) method, which combines microfluidics-based protein purification with cryo-EM grid preparation, cryo-EM structures of soluble bacterial and eukaryotic membrane proteins can be solved starting from less than 1 µg of a target protein and progressing from cells to cryo-EM grids within a few hours. This scales down the amount of starting biological material hundreds to thousands of times, opening possibilities for the structural characterization of hitherto inaccessible proteins.
External links	Nat Methods / PubMed:41233542
Methods	EM (single particle)
Resolution	2.2 - 3.51 Å
Structure data	52333 9hpl EMDB-52333, PDB-9hpl: E. coli beta-galactosidase labeled with Chromeo P503 dye purified using MISO Method: EM (single particle) / Resolution: 2.3 Å 52334 9hpm EMDB-52334, PDB-9hpm: E. coli beta-galactosidase labeled with Chromeo P503 dye purified using MISO from 1ug Method: EM (single particle) / Resolution: 2.2 Å 52344 9hqn EMDB-52344, PDB-9hqn: Cryo-EM structure of bovine TMEM206 Method: EM (single particle) / Resolution: 2.86 Å 52345 9hqo EMDB-52345, PDB-9hqo: Cryo-EM structure of bovine TMEM206-YFP purified and plunged using MISO (micro-purification) Method: EM (single particle) / Resolution: 2.97 Å 52346 9hqp EMDB-52346, PDB-9hqp: Cryo-EM structure of mouse TMEM16F-YFP purified and plunged using MISO (microfluidic isolation) Method: EM (single particle) / Resolution: 3.51 Å EMDB-52486: Cryo-EM structure of TRPC6 (complete particle) purified and plunged using MISO (micro-purification) Method: EM (single particle) / Resolution: 3.49 Å EMDB-52487: Cryo-EM structure of TRPC6 (extra cellular domain) purified and plunged using MISO (micro-purification) Method: EM (single particle) / Resolution: 3.44 Å
Chemicals	ChemComp-HOH: WATER ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-CA: Unknown entry
Source	Escherichia coli (E. coli) escherichia coli k-12 (bacteria) bos taurus (domestic cattle) mus musculus (house mouse) aequorea victoria (jellyfish) unidentified (others)
Keywords	HYDROLASE / Glycosyl hydrolase / MEMBRANE PROTEIN / Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH / pH-gated chloride channel / lipid scramblase