The recombinant Kunitz-type domain (C5) of human collagen cr3(VI) chain was previously described at 1.6 ,A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2,~ resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2,4,. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (Xl = -60°) • The solvent molecules and a phosphate ion are well ordered with an average B of 38 ~2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.
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