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A new crystal structure of linear diubiquitin adopts a compact conformation that differs from its previously reported extended conformation.

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The 1.75 Å resolution X-ray crystallographic structure of human evectin-2 pleckstrin homology domain revealed ligand-induced conformational change. This structural change effectively explains the strict phospholipid binding specificity.

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A comparative analysis of sulfur phasing of death receptor 6 (DR6) using data collected at wavelengths of 2.0 and 2.7 Å is presented. SAXS analysis of unliganded DR6 defines a dimer as the minimum physical unit in solution.
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