Crystalline bovine liver catalase

Structure and heme environment of beef liver catalase at 2.5 A resolution.

“…This information was used in a vector search (44) procedure to locate two major heavy atom sites, A and B, and the molecular center (0,SY,5/6). The latter was determined to be at Sy = 0.65 and is therefore within the limits of0.56 < Sy -0.72 estimated by Eventoffet al (37). The presence oftwo major heavy atom sites, susceptible to mercurial substitution, is consistent with two highly reactive sulfhydryl groups per subunit in beef liver catalase (45).…”

“…However, approximately two of the four heme groups are degraded to a high-spin Fe(III)-biliverdin complex (20,21 Catalase was one of the first enzymes to be crystallized (20). Electron microscopy (23,24), electron diffraction (25)(26)(27), and low angle x-ray scattering (28) all show a slightly ellipsoidal molecule with an average radius of 40 A. Single-crystal forms of catalase reported to date (29)(30)(31)(32)(33)(34)(35)(36)(37) contain one or more molecules per asymmetric unit except for bacterial catalase (35), the catalase ofPenicillium vitale (36), and a trigonal form ofbeefliver catalase (37), all ofwhich incorporate one crystallographic 2-fold axis in the molecule. We describe here the preliminary results of a high-resolution structure determination of the beef liver catalase crystals reported by Eventoff et al (37).…”

The refined structure of beef liver catalase at 2·5 Å resolution

“…Each subunit has usually 506 amino acids, although some beef liver extracts have been reported with 10 to 15 additional residues (Schroeder, Shelton, Shelton, Robberson, Apell, Fang & Bonaventura, 1982;Schroeder, Shelton, Shelton, Apell, Evans, Bonaventura & Fang, 1982). The crystals are trigonal, have space group P3221 with a = 142.0 and c = 103.7 A and were first reported by Eventoff, Tanaka & Rossmann (1976). The molecule is positioned on a crystallographic diad with two subunits per crystallographic asymmetric unit.…”

Sixty years from discovery to solution: crystal structure of bovine liver catalase form III

“…Additionally, the unit-cell parameters of very thin plates of a second P2 1 2 1 2 1 form were determined to be a = 69, b = 173.5, c = 206 Å through both EM and X-ray powder diffraction (Unwin, 1975). Finally, in 1976, a second distinct P3 1 21 or P3 2 21 trigonal form was discovered by Rossmann and Eventoff, with unit-cell parameters a = b = 142.3 (6), c = 104.0 (5) Å (Eventoff et al, 1976).…”