Purification and crystallographic analysis of a novel cold‐ active esterase (HaEst1) from halocynthiibacter arcticus

This report deals with the purification, characterization, and a preliminary crystallographic study of a novel cold‐active esterase (HaEst1) from Halocynthiibacter arcticus. Primary sequence analysis reveals that HaEst1 has a catalytic serine in G‐x‐S‐x‐G motif. The recombinant HaEst1 was cloned, expressed, and purified. SDS‐PAGE and zymographic analysis were carried out to characterize the properties of HaEst1. A single crystal of HaEst1 was obtained in a solution containing 10% (w/v) PEG 8000/8% ethylene glycol, 0.1 M Hepes‐NaOH, pH 7.5. Diffraction data were collected to 2.10 Å resolution with P21 space group. The final Rmerge and Rp.i.m values were 7.6% and 3.5% for 50‐2.10 Å resolution. The unit cell parameters were a = 35.69 Å, b = 91.21 Å, c = 79.15 Å, and β = 96.9°.