Crystallization and preliminary X-ray analysis of methionine aminopeptidase from the hyperthermophilic bacterium Pyrococcus furiosus

Methionine aminopeptidase (MAP) from Pyrococcus furiosus (Pfu) has been crystallized in four different forms (A, B, C and D). Form A crystals belong to space group P21 with unit‐cell dimensions a = 54.18, b = 85.72, c = 72.84 Å, β = 108.34°. Forms B, C and D belong to space group P62(4) with unit‐cell dimensions a = 139.1, c = 63.7 Å for form B, a = 198.6, c = 243.8 Å for form C, and a = 111.0, c = 125.0 Å for form D. Forms A and D diffract to 2.9 Å, form B diffracts to 3.5 Å, and form C crystals diffract to 4.5 Å. Form A contains two molecules of MAP‐Pfu per asymmetric unit. The binuclear metal center positions and a non‐crystallographic twofold symmetry matrix has been determined for the form A crystals.