Summary for 5NI1
| Entry DOI | 10.2210/pdb5ni1/pdb |
| EMDB information | 3488 |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | volta phase plate, single particle analysis, hemoglobin, oxygen transport |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64547.05 |
| Authors | Khoshouei, M.,Radjainia, M.,Bunker, R.,Baumeister, W.,Danev, R. (deposition date: 2017-03-22, release date: 2017-04-12, Last modification date: 2024-05-08) |
| Primary citation | Khoshouei, M.,Radjainia, M.,Baumeister, W.,Danev, R. Cryo-EM structure of haemoglobin at 3.2 angstrom determined with the Volta phase plate. Nat Commun, 8:16099-16099, 2017 Cited by 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 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. PubMed: 28665412DOI: 10.1038/ncomms16099 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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