issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

October 2010 issue

Highlighted illustration

Cover illustration: A pair of fusion proteins forming a dimer through GFP-GFP interaction are coloured as magenta/green or cyan/yellow (p. 1059). The C-terminal ubiquitin moiety extends away from the N-terminal GFP moiety and interacts with the peripheral loops of the GFP moiety of another molecule.

research papers

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The crystal structures of complexes of octahaem cytochrome c nitrite reductase from the bacterium T. nitratireducens (TvNiR) with sulfite and cyanide are reported. The sulfite reductase activity of TvNiR is quantitatively characterized.

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Crystallographic and molecular-dynamics studies indicate a possible relation between variations in oligomerization and in stability, in addition to providing insights into changes in subunit structure on oligomerization.

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The GFP-fusion technique has been successfully applied to the crystallization of small proteins and domains, using ubiquitin and the ubiquitin-binding motif as test cases.

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C. perfringens α-toxin variant T74I has been shown to have significantly reduced cytotoxicity. Here, further characterization of the activity of this variant and its X-ray crystallographic structure are presented.

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Radiation damage to protein crystals exhibits two regimes of temperature-activated behavior between T = 300 and 100 K, with a crossover at the protein glass transition near 200 K. These results have implications for mechanistic studies of proteins and for structure determination when cooling to T = 100 K creates excessive disorder.

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Structures of the Grb2 SH2 domain complexed with a series of flexible and constrained replacements of the phosphotyrosine residue in tripeptides derived from Ac-pYXN (where X = V, I, E and Q) were compared to determine what, if any, structural differences arise as a result of ligand preorganization.

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