Preliminary analysis of crystals of 4-oxalocrotonate tautomerase, an enzyme composed of unusually small monomers.
Crystals of 4-oxalocrotonate tautomerase have been obtained by the vapor-diffusion method using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 118.1, b = 95.6, c = 97.4, alpha = beta = gamma = 90 degrees and diffract well to at least 2.7 A resolution. There are approximately ten 6811 dalton subunits of the enzyme per asymmetric unit, giving a crystal solvent content of 70%.
Department of Chemistry, Boston University, MA 02215.
R C
RC
Davenport
C P
CP
Whitman
D003460:Crystallization; D007535:Isomerases / Q000737:chemistry*; D016958:Pseudomonas putida / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; C021918:4-oxalocrotonate tautomerase; D007535:Isomerases