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Crystallization and preliminary X-ray analysis of a cold-active ?-galactosidase from the psychrotrophic and halotolerant Planococcus sp. L4.


ABSTRACT: ?-Galactosidases catalyze the hydrolysis of a galactosyl moiety from the nonreducing termini of oligosaccharides or from glycosides. A novel GH family 42 cold-active ?-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, ? = 62.66, ? = 69.48, ? = 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.

SUBMITTER: Zhang L 

PROVIDER: S-EPMC3151126 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of a cold-active β-galactosidase from the psychrotrophic and halotolerant Planococcus sp. L4.

Zhang Liping L   Wang Kui K   Mo Zhongxing Z   Liu Yuhuan Y   Hu Xiaopeng X  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110720 Pt 8


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  ...[more]

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