6CLA

2.80 A MicroED structure of proteinase K at 6.0 e- / A^2

Summary for 6CLA

• Entry DOI: 10.2210/pdb6cla/pdb
• EMDB information: 7490 7491 7492 7493 7494
• Descriptor: Proteinase K (1 entity in total)
• Functional Keywords: hydrolase
• Biological source: Parengyodontium album (Engyodontium album, Tritirachium album)
• Total number of polymer chains: 1
• Total formula weight: 28930.78

Authors

Hattne, J.,Shi, D.,Glynn, C.,Zee, C.-T.,Gallagher-Jones, M.,Martynowycz, M.W.,Rodriguez, J.A.,Gonen, T. (deposition date: 2018-03-02, release date: 2018-05-16, Last modification date: 2024-10-16)

Primary citation

Hattne, J.,Shi, D.,Glynn, C.,Zee, C.T.,Gallagher-Jones, M.,Martynowycz, M.W.,Rodriguez, J.A.,Gonen, T.
Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.
Structure, 26:759-766.e4, 2018

PubMed Abstract: Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data.

PubMed: 29706530
DOI: 10.1016/j.str.2018.03.021

Experimental method

ELECTRON CRYSTALLOGRAPHY (2.8 Å)