Related Experiment Video
Updated: Aug 11, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from
Marcelo E Guerin1, Alejandro Buschiazzo, Jana Korduláková
1Unité de Biochimie Structurale, CNRS URA 2185, Institut Pasteur, 75724 Paris Cedex 15, France.
Abstract:
Phosphatidylinositol mannosyltransferase (PimA) is an essential enzyme for mycobacterial growth that catalyses the first mannosylation step in phosphatidyl-myo-inositol mannoside (PIM) biosynthesis. The enzyme belongs to the large GT4 family of glycosyltransferases, for which no structure is currently available. Recombinant purified PimA from Mycobacterium smegmatis has been crystallized in the presence of GDP and myo-inositol. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.2, b = 72.4, c = 138.2 A, and diffract to 2.4 A resolution.
More Related Videos
13:34Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
10:45Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021