Solution structure of phosphorylase kinase studied using small-angle X-ray and neutron scattering.
Small-angle X-ray and neutron scattering have been used to characterize the solution structure of rabbit skeletal phosphorylase kinase. The radius of gyration of the unactivated holoenzyme determined from neutron scattering is 94 A, and its maximum dimension is approximately 275-295 A. A planar model has been constructed that is in general agreement with the dimensions of the transmission electron microscope images of negatively stained phosphorylase kinase and that gives values for the radius of gyration, maximum linear dimension, and a pair distribution function for the structure that are consistent with the scattering data.
Henderson
S J
SJ
Life Sciences Division, Los Alamos National Laboratory, New Mexico 87545.
Newsholme
P
P
Heidorn
D B
DB
Mitchell
R
R
Seeger
P A
PA
Walsh
D A
DA
Trewhella
J
J
D000818:Animals; D004789:Enzyme Activation; D008958:Models, Molecular; D009502:Neutrons; D010764:Phosphorylase Kinase / Q000737:chemistry* / Q000528:radiation effects; D011817:Rabbits; D012542:Scattering, Radiation; D012996:Solutions; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D012996:Solutions; D010764:Phosphorylase Kinase