Structure of catalase determined by MicroED

Author:

Nannenga Brent L1,Shi Dan1,Hattne Johan1ORCID,Reyes Francis E1,Gonen Tamir1

Affiliation:

1. Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States

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 (<xref ref-type="bibr" rid="bib26">Shi et al., 2013</xref>). 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.

Funder

Howard Hughes Medical Institute

Publisher

eLife Sciences Publications, Ltd

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

Reference32 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallographica Section D, Biological Crystallography,2010

2. The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals;Baker;Journal of Structural Biology,2010

3. iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM;Battye;Acta Crystallographica Section D, Biological Crystallography,2011

4. Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT;Blanc;Acta Crystallographica Section D, Biological Crystallography,2004

5. MolProbity: all-atom structure validation for macromolecular crystallography;Chen;Acta Crystallographica Section D, Biological Crystallography,2010

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