title: Diffraction quality crystals of lysin from spermatozoa of the red abalone (Haliotis rufescens).
abstract: Single crystals of the protein lysin (Mr = 16,070) from the spermatozoa of the red abalone (Haliotis rufescens) have been obtained by the vapor diffusion technique, using as precipitants a 32.5% saturated solution of (NH4)2SO4 (incubation at 18 degrees C) or a 5% w/v polyethyleneglycol 8000 solution (incubation at 29 degrees C), both in Bis-Tris-iminodiacetic acid buffers of pH 7.0. The addition to the droplets of EDTA, other carboxylate-containing polyanions, and/or organic solvents improved the size and quality of the crystals and, especially with (NH4)2SO4, addition of EDTA, and/or organic solvents produced a change in crystal habit which resulted in crystals more elongated in the b direction. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with a = 52.3 A, b = 46.0 A, and c = 81.5 A and one molecule per asymmetric unit. The crystals diffract to 2.3 A resolution. The molecular structure of lysin is relevant to the nonenzymatic mechanism by which the protein dissolves a hole in the egg vitelline layer during fertilization.
authors.affiliation: Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
authors.forename: M L
authors.initials: ML
authors.lastname: Baginsky
authors.forename: C D
authors.initials: CD
authors.lastname: Stout
authors.forename: V D
authors.initials: VD
authors.lastname: Vacquier
mesh_terms: D000818:Animals; D003460:Crystallization; D004492:Edetic Acid; D004798:Enzymes; D005399:Fishes; D008297:Male; D008970:Molecular Weight; D009088:Mucoproteins / Q000302:isolation & purification; D012997:Solvents; D013094:Spermatozoa / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D004798:Enzymes; D009088:Mucoproteins; D012997:Solvents; C010393:lysin, gastropoda; D004492:Edetic Acid