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The hyperthermostable endocellulase from P. furiosus was crystallized at pH 5.5. The new crystal form has symmetry consistent with space group C2 and exhibits a structure different from that of the protein crystallized at pH 9.0.

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A feruloyl esterase from T. cellulolyticus containing a carbohydrate-binding module was prepared, purified and crystallized. The crystal diffracted to 2.60 Å resolution using synchrotron radiation.

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Acetylxylan esterase from T. cellulolyticus expressed as a truncated form without the cellulose-binding module 1 domain was purified and crystallized. The crystal diffracted to 1.50 Å resolution using synchrotron radiation.
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