PMID:15039577
| Citation |
Van Straaten, KE, Dijkstra, BW and Thunnissen, AM (2004) Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:758-60 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1107/S0907444904002574 |
| Keywords |
Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Glycosyltransferases/chemistry; Mutation; Solubility |
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