Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli
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Updated: Feb 12, 2026

Scalable Isolation and Purification of Extracellular Vesicles from Escherichia coli and Other Bacteria
Published on: October 13, 2021
Karin E Van Straaten1, Bauke W Dijkstra, Andy Mark W H Thunnissen
1Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Abstract:
The lytic transglycosylase MltA from Escherichia coli with its membrane anchor and signal sequence deleted has been purified to homogeneity by means of cation-exchange chromatography. The enzyme was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 103.70, c = 109.84 A and one molecule per asymmetric unit. Crystals diffract to 2.2 A resolution on a synchrotron-radiation source.
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