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Structure of catalase determined by MicroED

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...

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Published in:eLife 2014-10, Vol.3, p.e03600-e03600
Main Authors: Nannenga, Brent L, Shi, Dan, Hattne, Johan, Reyes, Francis E, Gonen, Tamir
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description 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.
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subjects Animals
Biochemistry
Biophysics and Structural Biology
Catalase
Catalase - chemistry
Cattle
cryo EM
Crystallography
Crystals
Databases, Protein
Datasets
Diffraction
Electron diffraction
electron microscopy
Ligands
Liver
Lysozyme
micro crystal
MicroED
Models, Molecular
Quality
Reproducibility of Results
Research Advance
Single crystals
Static Electricity
X-ray crystallography
X-Ray Diffraction - methods
title Structure of catalase determined by MicroED
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