Structure of the dihydrolipoamide succinyltransferase catalytic domain fromEscherichia coliin a novel crystal form: a tale of a common protein crystallization contaminant

Volume: 75, Issue: 9, Pages: 616 - 624
Published: Aug 29, 2019
Abstract
The crystallization of amidase, the ultimate enzyme in the Trp-dependent auxin-biosynthesis pathway, from Arabidopsis thaliana was attempted using protein samples with at least 95% purity. Cube-shaped crystals that were assumed to be amidase crystals that belonged to space group I4 (unit-cell parameters a = b = 128.6, c = 249.7 Å) were obtained and diffracted to 3.0 Å resolution. Molecular replacement using structures from the PDB containing the...
Paper Details
Title
Structure of the dihydrolipoamide succinyltransferase catalytic domain fromEscherichia coliin a novel crystal form: a tale of a common protein crystallization contaminant
Published Date
Aug 29, 2019
Volume
75
Issue
9
Pages
616 - 624
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