Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate

Maryam Khoshouei, Mazdak Radjainia, Wolfgang Baumeister and Radostin Danev ()
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Maryam Khoshouei: Max Planck Institute of Biochemistry
Mazdak Radjainia: The Clive and Vera Ramaciotti Centre for Cryo-EM, Monash University
Wolfgang Baumeister: Max Planck Institute of Biochemistry
Radostin Danev: Max Planck Institute of Biochemistry

Nature Communications, 2017, vol. 8, issue 1, 1-6

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms16099

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