Expression, purification and preliminary X-ray diffraction analysis of the catalytic module of a β-agarase from the flavobacterium Zobellia galactanivorans

A novel family GH16 β-agarase from the marine bacterium Zobellia galactanivorans was expressed, purified and crystallized. Hexagonal crystals belonging to space group P3₁21 diffracted to 2.2 Å resolution, whereas orthorhombic crystals belonging to space group P2₁2₁2₁ diffracted to 1.5–Å resolution. Marine bacteria secrete specific glycoside hydrolases such as agarases to access polysaccharides from algal cell walls as a carbon and energy source. In an attempt to identify agarases with variable degradation patterns, a novel family GH16 β-agarase from the marine bacterium Zobellia galactanivorans was expressed, purified and crystallized. The purified enzyme crystallized in two distinct forms that were grown by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. Hexagonal crystals belonging to space group P3₁21 diffracted to 2.2 Å resolution, whereas orthorhombic crystals belonging to space group P2₁2₁2₁ diffracted to 1.5 Å resolution