SynopsisThe crystal structure and conformation of the synthetic cyclic tetrapeptide, cyclo(L-Pro-Sar)z, was determined by x-ray analysis. The peptide crystallizes in the orthorhombic space group P21212~ with cell parameters a = 9.277(1), b = 12.884(1), and c = 15.581(2) A. The crystal structure was solved by the symbolic addition procedure for direct phase determination and least-squares refinement using 1796 reflections, which led to the final R value of 0.043. This structure provides the first example observed in a crystal of a cyclic tetrapeptide in which all four peptide units have been found in the cis conformation with w angles deviating slightly by 2"-10" from the ideal value of 0". It was also found that the two Pro C"-CO single bonds assumed a trans' ($ = 159.6" and 158.4") conformation. Adjoining average planes of the peptide groups fall at nearly right angles to each other. The pyrrolidine ring conformations of the two prolyl residues are in the envelope form, with Cr carbon out of the least-squares planes for the remaining four atoms.