6SHT

Molecular structure of mouse apoferritin resolved at 2.7 Angstroms with the Glacios cryo-microscope

Summary for 6SHT

• Entry DOI: 10.2210/pdb6sht/pdb
• EMDB information: 0144 0263 10101 10205 20026 20027 20155 20225 20227 20228 20229 3853 4213 4698 4701 4905 6800 6802 8428 9599 9865 9890 9914
• Descriptor: Ferritin heavy chain, FE (III) ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: apoferritin, iron binding, iron storing, complex, metal binding protein
• Biological source: Mus musculus (House mouse)
• Total number of polymer chains: 1
• Total formula weight: 21177.78

Authors

Hamdi, F.,Tueting, C.,Semchonok, D.,Kyrilis, F.,Meister, A.,Skalidis, I.,Schmidt, L.,Parthier, C.,Stubbs, M.T.,Kastritis, P.L. (deposition date: 2019-08-08, release date: 2020-05-13, Last modification date: 2024-05-22)

Primary citation

Hamdi, F.,Tuting, C.,Semchonok, D.A.,Visscher, K.M.,Kyrilis, F.L.,Meister, A.,Skalidis, I.,Schmidt, L.,Parthier, C.,Stubbs, M.T.,Kastritis, P.L.
2.7 angstrom cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope.
Plos One, 15:e0232540-e0232540, 2020

PubMed Abstract: Here we present the structure of mouse H-chain apoferritin at 2.7 Å (FSC = 0.143) solved by single particle cryogenic electron microscopy (cryo-EM) using a 200 kV device, the Thermo Fisher Glacios®. This is a compact, two-lens illumination system with a constant power objective lens, without any energy filters or aberration correctors, often thought of as a "screening cryo-microscope". Coulomb potential maps reveal clear densities for main chain carbonyl oxygens, residue side chains (including alternative conformations) and bound solvent molecules. We used a quasi-crystallographic reciprocal space approach to fit model coordinates to the experimental cryo-EM map. We argue that the advantages offered by (a) the high electronic and mechanical stability of the microscope, (b) the high emission stability and low beam energy spread of the high brightness Field Emission Gun (X-FEG), (c) direct electron detection technology and (d) particle-based Contrast Transfer Function (CTF) refinement have contributed to achieving high resolution. Overall, we show that basic electron optical settings for automated cryo-electron microscopy imaging can be used to determine structures approaching atomic resolution.

PubMed: 32374767
DOI: 10.1371/journal.pone.0232540

Experimental method

ELECTRON MICROSCOPY (2.73 Å)