Crystal structure of human arginase I in complex with difluoromethylornithine (DFMO)

Binding of alpha,alpha-Disubstituted Amino Acids to Arginase Suggests New Avenues for Inhibitor Design

14% JEFFAMINE 2001, 0.1M HEPES PH 7.0, 50MM BICINE PH 8.5, 1.4MM TYMINE, VAPOR DIFFUSION, HANGING DROP

Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution

Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A

STRUCTURE IS AFFECTED BY PERFECT HEMIHEDRAL TWINNING. THE SUBMITTED INTENSITIES DATA ARE UNTWINNED, AND HAVE BEEN USED AS SUCH DURING THE REFINEMENT. THE TWINNING FACTOR IS -H,-K,L AND THE TWIN FRACTION IS = 0.5

DFMO binding, polyamine biosynthesis, HYDROLASE-HYDROLASE INHIBITOR complex