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Updated: Oct 12, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary X-ray investigation of uridine phosphorylase from Escherichia coli
Abstract:
Crystals of uridine phosphorylase from Escherichia coli K12 have been grown from solutions of polyethylene glycol 4000. The crystals are trigonal, space group R3; the hexagonal axes are a = 154.4 A and c = 49.4 A. The crystals are quite stable to x-rays and diffract beyond 2.6 A resolution. It appears that the molecule is a hexamer with a subunit molecular weight of 27,500 and utilizes the 3-fold symmetry of the space group, resulting in two subunits/asymmetric unit.
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