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The structure of calcium-depleted human C-reactive protein has been determined at 3.15 Å from perfectly twinned crystals. The structure reveals two independent pentamers which form a face-to-face decamer across a dyad near-parallel to the twinning twofold axis.

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An atomic resolution structure of the NAD+ synthetase is presented with implications for the catalytic mechanism.
Keywords: NAD+ synthetase.

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An introductory report of the ICCBM9 meeting in Jena, Germany, 2002, is given.

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The crystallization conditions of the synthetic RNA duplex r(GCGGCGU)•r(GCGCCGC), part of the Thermus flavus 5S rRNA domain B, were investigated in detail. The crystallization analysis revealed a relativ narrow crystallization zone. Single sequence variations did not enhance the crystal quality, however the crystallization under microgravity provided crystals of higher quality. They belong to the space group P3121 with unit cell dimensions of a = b = 35.0 Å and c = 141.2 Å. Diffraction data up to 2.6 Å were collected and the structure subsequently analysed and refined to an R-value of 22.4 %. The conformation of the two molecules in the asymmetric unit is stabilized by intermolecular hydrogen bonds. The two molecules A and B are perpendicular to each other and interacting head to tail with symmetry related molecules. They form pseudo-continuous infinite helices in the crystal lattice.

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The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album in complex with adenine has been refined to 1.9 Å resolution. High quality crystals of the ML-I complex were obtained by the method of vapour diffusion using the high density protein crystal growth system (HDPCG) on the international space station, mission ISS 6A. Hexagonal crystals were grown during three months under microgravity conditions. Diffraction data to 1.9Å were collected applying synchrotron radiation and cryo- techniques. The structure was refined subsequently to analyse the structure of ML-I and particularly the active site conformation, complexed by adenine that mimics the RNA substrate binding.
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