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The wild-type protein and four active-site mutants of xylanase II from Trichoderma reesei that catalyzes the hydrolysis of glycosidic bonds in xylan have successfully been crystallized. The crystallization of several structures including ligand-free and protein ligand complexes containing the substrate (xylohexaose) or product (xylotriose) are detailed.

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The complex of the abscisic acid receptor PYL3 with (-)-ABA was crystallized and refined to obtain high-quality diffraction data. Diffraction data were collected and processed at 2.65 Å resolution.
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