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Updated: May 30, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary X-ray analysis of a cold-active β-galactosidase from the psychrotrophic and
Liping Zhang1, Kui Wang, Zhongxing Mo
1School of Pharmaceutical Sciences, Sun Yat-sen University, Higher Education Mega Center, Guangzhou, Guangdong, People's Republic of China.
Abstract:
β-Galactosidases catalyze the hydrolysis of a galactosyl moiety from the nonreducing termini of oligosaccharides or from glycosides. A novel GH family 42 cold-active β-galactosidase identified from the psychrotrophic and halotolerant Planococcus sp. L4 (BgaP) was crystallized and a complete data set was collected from a single frozen crystal on an in-house X-ray source. The crystal diffracted to 2.8 Å resolution and belonged to space group P1, with unit-cell parameters a = 104.29, b = 118.12, c = 121.12 Å, α = 62.66, β = 69.48, γ = 70.74°. A likely Matthews coefficient of 2.58 Å(3) Da(-1) and solvent content of 52.32% suggested the presence of six protein subunits in the asymmetric unit.
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