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Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Brevibacterium fuscum
C A Earhart1, R Radhakrishnan, A M Orville
1Department of Biochemistry, University of Minnesota Medical School, Minneapolis 55455.
Journal of Molecular Biology
|February 11, 1994
Abstract:
The enzyme protocatechuate 3,4-dioxygenase from the Gram positive organism Brevibacterium fuscum crystallizes in the triclinic space group P1 with unit cell dimensions a = 96.1 A, b = 97.2 A, c = 118.1 A and alpha = 113.9 degrees, beta = 90.7 degrees, gamma = 117.8 degrees. The rod-like crystals diffract to 2.4 A resolution. Rotation function analysis suggests that there are six promoters arranged with local 32 symmetry in the asymmetric unit rather than the previously proposed pentameric complex.