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Two crystal structures of a plant endo-1,3-β-glucanase representing glycoside hydrolase family GH17 in complexes with products of laminarahexose hydrolysis reveal the protein–saccharide interactions at five key binding subsites for the first time. A trisaccharide is bound at subsites −3, −2 and −1 of the nonreducing end (glycon portion) in both structures, and in one structure an extra tetrasaccharide is bound at subsites +1 to +4 of the reducing end (aglycon portion).

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Ultrahigh-resolution crystal structures of metal complexes of self-complementary Z-DNA with the sequence d(CG)3 revealed different coordination patterns for Mn2+ (octahedral) and Zn2+ (octahedral and tetrahedral) cations. The complete sperminium cation is visible in electron density in the Mn2+ structure, while in the Zn2+ structure it is partly disordered in unison with fragments of the DNA molecule.
Keywords: Z-DNA; d(CG)3; Mn2+; Zn2+.

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The policy of the Protein Data Bank that the first deposition of a small-molecule ligand, even with erroneous atom numbering, sets a precedent over accepted nomenclature rules is disputed.

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The crystal structure of a complex of two mulberry silkworm storage proteins, SP2 and SP3, has been determined. The presence of two different proteins in the native complex was detected crystallographically according to electron-density maps.

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The crystal structures of complexes of M. truncatula nodulin 13 with four cytokinins, trans-zeatin, N6-isopentenyladenine, kinetin and N6-benzyladenine, show an unusual mode of dimerization of this PR-10-fold plant protein. The cytokinin-binding mode in the internal cavity of the protein is the same in each complex and resembles the pattern found in the cytokinin receptor protein.
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