WikiSysop: Created page with "== Citation == Eluru, G., De Gieter, S., Schenck, S., Stroobants, A., Shrestha, B., Erbel, P., Brunner, J.D. and Efremov, R.G. 2025. MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Nature methods. (2025), 1–11. == Abstract == Single-particle cryogenic electron microscopy (cryo-EM) enables reconstruction of atomic-resolution 3D maps of proteins by visualizing thousands to millions of purified pro..."

2026-04-23T07:07:30Z

Created page with "== Citation == Eluru, G., De Gieter, S., Schenck, S., Stroobants, A., Shrestha, B., Erbel, P., Brunner, J.D. and Efremov, R.G. 2025. MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Nature methods. (2025), 1–11. == Abstract == Single-particle cryogenic electron microscopy (cryo-EM) enables reconstruction of atomic-resolution 3D maps of proteins by visualizing thousands to millions of purified pro..."

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== Citation ==

Eluru, G., De Gieter, S., Schenck, S., Stroobants, A., Shrestha, B., Erbel, P., Brunner, J.D. and Efremov, R.G. 2025. MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Nature methods. (2025), 1–11.

== 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 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.

== Keywords ==

== Links ==

https://www.nature.com/articles/s41592-025-02894-x

== Related software ==

== Related methods ==

== Comments ==

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