EMD-3651
Cryo-EM asymmetric reconstruction of haemoglobin at 3.6 A determined with the Volta phase plate (subset of particles)
EMD-3651
Single-particle3.6 Å
Deposition: 24/03/2017Map released: 19/07/2017
Last modified: 19/07/2017
Sample Organism:
Homo sapiens
Sample: Hemoglobin
Deposition Authors: Khoshouei M, Radjainia M, Baumeister W, Danev R
Sample: Hemoglobin
Deposition Authors: Khoshouei M, Radjainia M, Baumeister W, Danev R
Cryo-EM structure of haemoglobin at 3.2 angstrom determined with the Volta phase plate.
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.
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.