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crystallization papers
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 P3121 or P3221, with unit-cell parameters a = b = 103.70, c = 109.84 Å and one molecule per asymmetric unit. Crystals diffract to 2.2 Å resolution on a synchrotron-radiation source.