The enzyme phosphoethanolamine transferase A is involved in the addition of phosphoethanolamine moieties to lipid A in Neisseria meningitidis. The enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain that is present in the periplasm of the bacteria. A membrane-deletion construct of the enzyme was designed and expressed in Escherichia coli. Well ordered crystals that diffracted to 1.7 Å resolution were obtained by carrying out a limited trypsin digestion of the protein to remove a predicted N-terminal disordered portion. The crystals belonged to space group P21, with unit-cell parameters a = 44.3, b = 71.6, c = 49.9 Å, [beta] = 109.2°, and contained one molecule in the asymmetric unit.
|Journal||ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS|
|Publication status||Published - 1 Dec 2012|
Anandan, A., Piek, S., Kahler, C., & Vrielink, A. (2012). Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 68(12), 1494-1497. https://doi.org/10.1107/S1744309112042236