| Summary: | This report deals with the purification, characterization, and a preliminary crystallographic study of a novel cold-active esterase (<i>Ha</i>Est1) from Halocynthiibacter arcticus. Primary sequence analysis reveals that <i>Ha</i>Est1 has a catalytic serine in G-x-S-x-G motif. The recombinant <i>Ha</i>Est1 was cloned, expressed, and purified. SDS-PAGE and zymographic analysis were carried out to characterize the properties of <i>Ha</i>Est1. A single crystal of <i>Ha</i>Est1 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 P2<sub>1</sub> space group. The final R<sub>merge</sub> and R<sub>p.i.m</sub> values were 7.6% and 3.5% for 50-2.10 Å resolution. The unit cell parameters were <i>a</i> = 35.69 Å, <i>b</i> = 91.21 Å, <i>c</i> = 79.15 Å, and = 96.9°.
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