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Crystallization and preliminary X-ray analysis of a novel halotolerant feruloyl esterase identified from a soil metagenomic library.

ABSTRACT: Feruloyl esterase cleaves the ester linkage formed between ferulic acid and polysaccharides in plant cell walls and thus has wide potential industrial applications. A novel feruloyl esterase (EstF27) identified from a soil metagenomic library was crystallized and a complete data set was collected from a single cooled crystal using an in-house X-ray source. The crystal diffracted to 2.9?Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 94.35, b = 106.19, c = 188.51?Å, ? = ? = ? = 90.00°. A Matthews coefficient of 2.55?Å(3)?Da(-1), with a corresponding solvent content of 51.84%, suggested the presence of ten protein subunits in the asymmetric unit.

SUBMITTER: Chen SK

PROVIDER: S-EPMC3388917 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of a novel halotolerant feruloyl esterase identified from a soil metagenomic library.

Chen Shang-ke SK Wang Kui K Liu Yuhuan Y Hu Xiaopeng X

Acta crystallographica. Section F, Structural biology and crystallization communications 20120627 Pt 7

Feruloyl esterase cleaves the ester linkage formed between ferulic acid and polysaccharides in plant cell walls and thus has wide potential industrial applications. A novel feruloyl esterase (EstF27) identified from a soil metagenomic library was crystallized and a complete data set was collected from a single cooled crystal using an in-house X-ray source. The crystal diffracted to 2.9 Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 94.35, b = 106.19, c = 18 ...[more]

PMID: 22750860

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