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A comparison of the binding site of mexicain for E-64 with those of other E-64–cysteine protease complexes shows that highly conserved interactions are replaced by other interactions in which water molecules play an essential role.

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The crystallographic structure of the N114A mutant of the SH3 domain of the Abelson leukaemia virus tyrosine kinase complexed with a high-affinity peptide is reported. An X-ray diffraction data set was collected directly from crystals from the initial screening using the capillary counter-diffusion technique.
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