structural communications
A protein-engineering study revealed that the C-terminal domain of a thermostable β-glucosidase contributes to its polymeric state.
structural communications
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.
crystallization communications
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.
crystallization communications
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.