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Updated: May 11, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Purification, crystallization and preliminary X-ray diffraction analysis of Omp6, a protoilludene synthase from
Maureen B Quin1, Grayson Wawrzyn, Claudia Schmidt-Dannert
1BMBB/BTI, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108, USA. mbquin@umn.edu
Abstract:
Basidiomycetes produce a wide range of industrially relevant natural products. One of the main classes of natural products isolated from fungi are terpenoids, a highly diverse group of secondary metabolites, many of which are bioactive and have been adapted for pharmaceutical purposes. The discovery of a suite of novel sesquiterpene synthases from Omphalotus olearius via genome sequencing and bioinformatic analyses has recently been described. Here, the expression, purification and crystallization of one of these enzymes (Omp6), a protoilludene synthase, is reported. A native crystal diffracted to a resolution of 2.9 Å and belonged to space group P21, with unit-cell parameters a = 43.67, b = 76.76, c = 107.22 Å, α = γ = 90, β = 95°. A diffraction data set was collected on a home-source Rigaku/MSC MicroMax-007 X-ray generator.

