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Updated: Aug 19, 2026
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary diffraction studies of thioesterase II from rat mammary gland
J L Buchbinder1, A Witkowski, S Smith
1Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448, USA.
Abstract:
Thioesterase II from rat mammary gland has been crystallized in the presence of decanoic acid by the vapor diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), and have cell dimensions, a = 52.7 A, b = 78.0 A, and c = 133.6 A. The asymmetric unit likely consists of two protein monomers based on predictions from its calculated Matthews coefficient. Crystals typically diffract to at least 2.5 A resolution and are suitable for X-ray crystallographic analysis.
