6nbb

Horse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 keVHorse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 keV

6nbb, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Structural highlights 6nbb is a 2 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Activity: Alcohol dehydrogenase, with EC number 1.1.1.1 Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Determining high-resolution structures of biological macromolecules amassing less than 100 kilodaltons (kDa) has been a longstanding goal of the cryo-electron microscopy (cryo-EM) community. While the Volta phase plate has enabled visualization of specimens in this size range, this instrumentation is not yet fully automated and can present technical challenges. Here, we show that conventional defocus-based cryo-EM methodologies can be used to determine high-resolution structures of specimens amassing less than 100 kDa using a transmission electron microscope operating at 200 keV coupled with a direct electron detector. Our ~2.7 A structure of alcohol dehydrogenase (82 kDa) proves that bound ligands can be resolved with high fidelity to enable investigation of drug-target interactions. Our ~2.8 A and ~3.2 A structures of methemoglobin demonstrate that distinct conformational states can be identified within a dataset for proteins as small as 64 kDa. Furthermore, we provide the sub-nanometer cryo-EM structure of a sub-50 kDa protein. High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM.,Herzik MA Jr, Wu M, Lander GC Nat Commun. 2019 Mar 4;10(1):1032. doi: 10.1038/s41467-019-08991-8. PMID:30833564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.