Related Experiment Videos
Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal
Morgunova EYu1, A M Mikhailov, A N Popov
1Institute of Crystallography of Russian Academy of Sciences, Moscow.
FEBS Letters
|June 26, 1995
Abstract:
Uridine phosphorylase from E. coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form. The structure was determined by the molecular replacement method at 2.5 A resolution. The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%. The amino acid fold of the protein was found to be the same as that in the trigonal crystals. The positions of flexible regions were refined. The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.