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Updated: Jul 31, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Direct methods in protein electron crystallography--beef liver catalase in its fully hydrated form at room
1Electron Diffraction Department, Hauptman-Woodward Medical Research Institute, Inc., Buffalo, New York 14203-1196, USA.
Abstract:
The crystal structure of beef liver catalase was determined ab initio in projection to 9 A resolution using electron diffraction data at room temperature from hydrated specimens maintained in an environmental chamber in the electron microscope. A conservative combination of symbolic addition with maximum entropy and likelihood led to a model with a Patterson correlation coefficient C = 0.89 to the observed data. This independent solution could then be compared favorably to a previous 23 A analysis of electron micrographs from frozen hydrated preparations. Prediction of the higher-resolution structure by extension of the lower-resolution image-based phase basis set also gave a good match to the direct-methods solution, particularly for the most intense reflections.
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