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TitleAtomic-resolution protein structure determination by cryo-EM.
Journal, issue, pagesNature, Vol. 587, Issue 7832, Page 157-161, Year 2020
Publish dateOct 21, 2020
AuthorsKa Man Yip / Niels Fischer / Elham Paknia / Ashwin Chari / Holger Stark /
PubMed AbstractSingle-particle electron cryo-microscopy (cryo-EM) is a powerful method for solving the three-dimensional structures of biological macromolecules. The technological development of transmission ...Single-particle electron cryo-microscopy (cryo-EM) is a powerful method for solving the three-dimensional structures of biological macromolecules. The technological development of transmission electron microscopes, detectors and automated procedures in combination with user-friendly image processing software and ever-increasing computational power have made cryo-EM a successful and expanding technology over the past decade. At resolutions better than 4 Å, atomic model building starts to become possible, but the direct visualization of true atomic positions in protein structure determination requires much higher (better than 1.5 Å) resolution, which so far has not been attained by cryo-EM. The direct visualization of atom positions is essential for understanding the mechanisms of protein-catalysed chemical reactions, and for studying how drugs bind to and interfere with the function of proteins. Here we report a 1.25 Å-resolution structure of apoferritin obtained by cryo-EM with a newly developed electron microscope that provides, to our knowledge, unprecedented structural detail. Our apoferritin structure has almost twice the 3D information content of the current world record reconstruction (at 1.54 Å resolution). We can visualize individual atoms in a protein, see density for hydrogen atoms and image single-atom chemical modifications. Beyond the nominal improvement in resolution, we also achieve a substantial improvement in the quality of the cryo-EM density map, which is highly relevant for using cryo-EM in structure-based drug design.
External linksNature / PubMed:33087927
MethodsEM (single particle)
Resolution1.15 - 1.56 Å
Structure data

11103

6z6u

EMDB-11103, PDB-6z6u:
1.25 A structure of human apoferritin obtained from Titan Mono-BCOR microscope
Method: EM (single particle) / Resolution: 1.25 Å

11121

6z9e

EMDB-11121, PDB-6z9e:
1.55 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope
Method: EM (single particle) / Resolution: 1.55 Å

11122

6z9f

EMDB-11122, PDB-6z9f:
1.56 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope
Method: EM (single particle) / Resolution: 1.56 Å

11668

7a6a

EMDB-11668, PDB-7a6a:
1.15 A structure of human apoferritin obtained from Titan Mono- BCOR microscope
Method: EM (single particle) / Resolution: 1.15 Å

11669

7a6b

EMDB-11669, PDB-7a6b:
1.33 A structure of human apoferritin obtained from Titan Mono- BCOR microscope
Method: EM (single particle) / Resolution: 1.33 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsMETAL BINDING PROTEIN / Apoferritin

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