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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 RHG XR XP 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 P21, with unit-cell parameters a = 91.50, b = 56.48, c = 146.35 Å, β = 110.01°, and in space group P1, with unit-cell parameters a = 55.51, b = 73.51 , c = 98.78 Å, α = 78.82, β = 77.65, γ = 67.73°, respectively. Diffraction data were collected at 100 K and the phases were determined using the molecular-replacement method. [ABSTRACT FROM AUTHOR]