Crystallization and preliminary crystallographic analysis of the major acid phosphatase from Legionella pneumophila.

ABSTRACT: The major acid phosphatase from Legionella pneumophila (LpMAP) belongs to the histidine acid phosphatase superfamily. It contains the characteristic histidine acid phosphatase (HAP) sequence motif RHGXRXP responsible for the hydrolysis of a phosphoryl group from phosphate monoesters under acidic conditions. Here, the crystallization and preliminary X-ray analysis of crystals of LpMAP in the apo form and in complex with L-(+)-tartrate are described. By using the hanging-drop vapour-diffusion method, apo LpMAP and LpMAP-tartrate were crystallized in space group P2(1), with unit-cell parameters a = 91.50, b = 56.48, c = 146.35 Å, ? = 110.01°, and in space group P1, with unit-cell parameters a = 55.51, b = 73.51, c = 98.78 Å, ? = 78.82, ? = 77.65, ? = 67.73°, respectively. Diffraction data were collected at 100 K and the phases were determined using the molecular-replacement method.

SUBMITTER: Zhou D 

PROVIDER: S-EPMC4461347 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature