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Crystallization and preliminary X-ray diffraction analysis of an endo-1,4-?-D-glucanase from Aspergillus aculeatus F-50.

ABSTRACT: Cellulose is the most abundant renewable biomass on earth, and its decomposition has proven to be very useful in a wide variety of industries. Endo-1,4-?-D-glucanase (EC 3.2.1.4; endoglucanase), which can catalyze the random hydrolysis of ?-1,4-glycosidic bonds to cleave cellulose into smaller fragments, is a key cellulolytic enzyme. An endoglucanase isolated from Aspergillus aculeatus F-50 (FI-CMCase) that was classified into glycoside hydrolase family 12 has been found to be effectively expressed in the industrial strain Pichia pastoris. Here, recombinant FI-CMCase was crystallized. Crystals belonging to the orthorhombic space group C222?, with unit-cell parameters a = 74.2, b = 75.1, c = 188.4?Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 1.6?Å resolution. Initial phase determination by molecular replacement clearly shows that the crystal contains two protein molecules in the asymmetric unit. Further model building and structure refinement are in progress.

SUBMITTER: Chen Y 

PROVIDER: S-EPMC4388172 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of an endo-1,4-β-D-glucanase from Aspergillus aculeatus F-50.

Chen Yun Y   Huang Jian Wen JW   Chen Chun Chi CC   Lai Hui Lin HL   Jin Jian J   Guo Rey Ting RT  

Acta crystallographica. Section F, Structural biology communications 20150320 Pt 4

Cellulose is the most abundant renewable biomass on earth, and its decomposition has proven to be very useful in a wide variety of industries. Endo-1,4-β-D-glucanase (EC 3.2.1.4; endoglucanase), which can catalyze the random hydrolysis of β-1,4-glycosidic bonds to cleave cellulose into smaller fragments, is a key cellulolytic enzyme. An endoglucanase isolated from Aspergillus aculeatus F-50 (FI-CMCase) that was classified into glycoside hydrolase family 12 has been found to be effectively expres  ...[more]

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