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TitleStructure of catalase determined by MicroED.
Journal, issue, pagesElife, Vol. 3, Page e03600, Year 2014
Publish dateOct 10, 2014
AuthorsBrent L Nannenga / Dan Shi / Johan Hattne / Francis E Reyes / Tamir Gonen /
PubMed AbstractMicroED 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 ...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.
External linksElife / PubMed:25303172 / PubMed Central
MethodsEM (electron crystallography)
Resolution3.2 Å
Structure data

6314

3j7b

EMDB-6314, PDB-3j7b:
Catalase solved at 3.2 Angstrom resolution by MicroED
Method: EM (electron crystallography) / Resolution: 3.2 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • bos taurus (domestic cattle)
KeywordsOXIDOREDUCTASE

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