Purification, crystallization and preliminary X‐ray diffraction analysis of the thiaminase type II from Staphylococcus aureus
Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4‐amino‐5‐hydroxymethyl‐2‐methylpyrimidine and 5‐(2‐hydroxyethyl)‐4‐methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour‐diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P212121 with unit‐cell parameters a = 103.5, b = 104.1, c = 109.6 Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85 Å3 Da−1. Initial attempts to solve the structure by molecular‐replacement techniques were successful.
No Supplementary Data
No Article Media