Fig. 2: CryoEM structures of various Hb species using the (an)aerobic chameleon protocol. | Nature Communications

Fig. 2: CryoEM structures of various Hb species using the (an)aerobic chameleon protocol.

From: Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification

Fig. 2: CryoEM structures of various Hb species using the (an)aerobic chameleon protocol.

A 2.55-Å resolution cryoEM structure of oxyHb determined under 25 µM NaDT. Zoomed-in views (shown below) of the α1 and β1 heme cofactors indicate a clear density of bound O2 above the Fe of each heme. B 2.52-Å resolution cryoEM structure of oxyHb determined under 5 mM NaDT. Zoomed-in views (shown below) of the α1 and β1 heme cofactors indicate a clear density of bound O2 above the Fe of each heme. C 2.72-Å resolution cryoEM structure of a partially oxygenated Hb species obtained under 20 mM NaDT. Clear O2 density was found above the α1 heme, while the α2, β1, and β2 heme groups lacked any such density. D 2.75-Å resolution cryoEM structure of deoxyHb under 60 mM NaDT. Orange and red α and β subunits have oxygen present, while blue subunits are deoxygenated.

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