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Updated: Oct 9, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic
1AIST-NIBHT CREST Centre of Structural Biology, 1-1 Higashi, Tsukuba 305-0046, Japan.
Abstract:
A protein belonging to the Lrp/AsnC transcription-factor family, pot1216151, from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In Escherichia coli, leucine-responsive protein (Lrp) and AsnC regulate a number of metabolic genes. The crystals of pot1216151 diffracted to 2.3 A using a conventional X-ray source and to 1.8 A using a synchrotron-radiation source. The space group was identified to be P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.9, c = 98.5 A. In combination with diffraction data obtained from K(2)[Pt(CN)(6)] and K(AuCl(4)) derivatives, an electron-density map was calculated at a resolution of 3.0 A. Four monomers were identified in the asymmetric unit, with four beta-strands and two alpha-helices in each monomer.
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