6XG6

Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3

Summary for 6XG6

• Entry DOI: 10.2210/pdb6xg6/pdb
• EMDB information: 22174
• Descriptor: Heat shock protein 75 kDa, mitochondrial, Fibronectin binding protein fusion, ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• Functional Keywords: hsp90, chaperone
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 175302.46

Authors

Liu, Y.X.,Wang, F.,Agard, D.A. (deposition date: 2020-06-17, release date: 2020-09-30, Last modification date: 2025-06-04)

Primary citation

Wang, F.,Liu, Y.,Yu, Z.,Li, S.,Feng, S.,Cheng, Y.,Agard, D.A.
General and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM.
Proc.Natl.Acad.Sci.USA, 117:24269-24273, 2020

PubMed Abstract: Affinity grids have great potential to facilitate rapid preparation of even quite impure samples in single-particle cryo-electron microscopy (EM). Yet despite the promising advances of affinity grids over the past decades, no single strategy has demonstrated general utility. Here we chemically functionalize cryo-EM grids coated with mostly one or two layers of graphene oxide to facilitate affinity capture. The protein of interest is tagged using a system that rapidly forms a highly specific covalent bond to its cognate catcher linked to the grid via a polyethylene glycol (PEG) spacer. Importantly, the spacer keeps particles away from both the air-water interface and the graphene oxide surface, protecting them from potential denaturation and rendering them sufficiently flexible to avoid preferential sample orientation concerns. Furthermore, the PEG spacer successfully reduces nonspecific binding, enabling high-resolution reconstructions from a much cruder lysate sample.

PubMed: 32913054
DOI: 10.1073/pnas.2009707117

Experimental method

ELECTRON MICROSCOPY (3.2 Å)