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The immunosuppressant cyclosporin-A (CsA) has been crystallized in complex with the bovine form of its major receptor protein cyclophilin (CyP) in three different forms by the hanging-drop vapor diffusion method. A hexagonal crystal form (P6(1)22 or P6(5)22; a = b = 110 A, c = 440 A) diffracts to 4 A resolution. Orthorhombic (P2(1)2(1)2(1) or P2(1)2(1)2; a = 154.3 A, b = 163.3 A, c = 94.7 A), and monoclinic (P2(1); a = 70.0 A, b = 162.5 A, c = 94.7, beta = 100.0 degrees) forms diffract to 2.2 A resolution. Self-rotation function analysis of the orthorhombic and monoclinic forms shows 52 point group local symmetry for both. A previously reported tetragonal crystal form of the complex also shares this local symmetry, suggesting that the observed motif may pre-exist in solution.