6ZEU
Crystal structure of proteinase K lamella by electron diffraction with a 50 micrometre C2 condenser aperture
This is a non-PDB format compatible entry.
Summary for 6ZEU
Entry DOI | 10.2210/pdb6zeu/pdb |
Descriptor | Proteinase K, CALCIUM ION (3 entities in total) |
Functional Keywords | protease, serine protease, hydrolase |
Biological source | Parengyodontium album (Tritirachium album) |
Total number of polymer chains | 1 |
Total formula weight | 28998.87 |
Authors | Evans, G.,Zhang, P.,Beale, E.V.,Waterman, D.G. (deposition date: 2020-06-16, release date: 2020-10-14, Last modification date: 2024-11-06) |
Primary citation | Beale, E.V.,Waterman, D.G.,Hecksel, C.,van Rooyen, J.,Gilchrist, J.B.,Parkhurst, J.M.,de Haas, F.,Buijsse, B.,Evans, G.,Zhang, P. A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction. Front Mol Biosci, 7:179-179, 2020 Cited by PubMed Abstract: MicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in thickness. Furthermore, traditional microED data processing uses established X-ray crystallography software that is not optimized for handling compound effects that are unique to electron diffraction data. Here, we present an integrated workflow for microED, from sample preparation by cryo-focused ion beam milling, through data collection with a standard Ceta-D detector, to data processing using the DIALS software suite, thus enabling routine atomic structure determination of protein crystals of any size and shape using microED. We demonstrate the effectiveness of the workflow by determining the structure of proteinase K to 2.0 Å resolution and show the advantage of using protein crystal lamellae over nanocrystals. PubMed: 32850967DOI: 10.3389/fmolb.2020.00179 PDB entries with the same primary citation |
Experimental method | ELECTRON CRYSTALLOGRAPHY (2.004 Å) |
Structure validation
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