3J7B
Catalase solved at 3.2 Angstrom resolution by MicroED
Summary for 3J7B
Entry DOI | 10.2210/pdb3j7b/pdb |
EMDB information | 6314 |
Descriptor | Catalase, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Bos taurus (bovine) |
Cellular location | Peroxisome: P00432 |
Total number of polymer chains | 4 |
Total formula weight | 245444.27 |
Authors | Nannenga, B.L.,Shi, D.,Hattne, J.,Reyes, F.E.,Gonen, T. (deposition date: 2014-06-09, release date: 2014-10-08, Last modification date: 2024-02-21) |
Primary citation | Nannenga, B.L.,Shi, D.,Hattne, J.,Reyes, F.E.,Gonen, T. Structure of catalase determined by MicroED. Elife, 3:e03600-e03600, 2014 Cited by PubMed Abstract: MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 Å resolution by MicroED. The data were collected by continuous rotation of the sample under constant exposure and were processed and refined using standard programs for X-ray crystallography. The ability of MicroED to determine the structure of bovine liver catalase, a protein that has long resisted atomic analysis by traditional electron crystallography, demonstrates the potential of this method for structure determination. PubMed: 25303172DOI: 10.7554/eLife.03600 PDB entries with the same primary citation |
Experimental method | ELECTRON CRYSTALLOGRAPHY (3.2 Å) |
Structure validation
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