Abstract
The core domain of a human histidine decarboxylase mutant was purified and cocrystallized with the inhibitor L-histidine methyl ester. Using synchrotron radiation, a data set was collected from a single crystal at 100 K to 1.8 Å resolution. The crystal belonged to space group C2, with unit-cell parameters a = 215.16, b = 112.72, c = 171.39 Å, β = 110.3°. Molecular replacement was carried out using the structure of aromatic L-amino-acid decarboxylase as a search model. The crystal contained three dimers per asymmetric unit, with a Matthews coefficient (V(M)) of 3.01 Å(3) Da(-1) and an estimated solvent content of 59.1%.