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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 |
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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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