+Search query
-Structure paper
Title | Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 8, Page 16099, Year 2017 |
Publish date | Jun 30, 2017 |
Authors | Maryam Khoshouei / Mazdak Radjainia / Wolfgang Baumeister / Radostin Danev / |
PubMed Abstract | With the advent of direct electron detectors, the perspectives of cryo-electron microscopy (cryo-EM) have changed in a profound way. These cameras are superior to previous detectors in coping with ...With the advent of direct electron detectors, the perspectives of cryo-electron microscopy (cryo-EM) have changed in a profound way. These cameras are superior to previous detectors in coping with the intrinsically low contrast and beam-induced motion of radiation-sensitive organic materials embedded in amorphous ice, and hence they have enabled the structure determination of many macromolecular assemblies to atomic or near-atomic resolution. Nevertheless, there are still limitations and one of them is the size of the target structure. Here, we report the use of a Volta phase plate in determining the structure of human haemoglobin (64 kDa) at 3.2 Å. Our results demonstrate that this method can be applied to complexes that are significantly smaller than those previously studied by conventional defocus-based approaches. Cryo-EM is now close to becoming a fast and cost-effective alternative to crystallography for high-resolution protein structure determination. |
External links | Nat Commun / PubMed:28665412 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.2 - 3.6 Å |
Structure data | EMDB-3488, PDB-5ni1: EMDB-3650: EMDB-3651: |
Chemicals | ChemComp-HEM: ChemComp-HOH: |
Source |
|
Keywords | OXYGEN TRANSPORT / Volta phase plate / Single particle analysis / Hemoglobin |