Crystallization and preliminary X-ray analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart.
Two crystal forms of bovine heart phosphotyrosyl protein phosphatase (BHPTP) have been examined by X-ray analysis. One crystal form grows as long rods with triclinic crystal symmetry and diffracts to 3 A resolution. The diffraction pattern of this form of the crystal shows twinning about a major axis. A second crystal form of BHPTP grows as flat trapezoidal prisms with monoclinic symmetry C2, and unit cell parameters a = 95.3 A, b = 43.3 A, c = 41.2 A and beta = 113.5 degrees. The unit cell dimensions indicate that there is one 18 kDa molecule per asymmetric unit. These crystals diffract to at least 2.2 A resolution and are resistant to decay in the X-ray beam.
Zhang
M
M
Department of Chemistry, Purdue University, West Lafayette, IN 47907.
Van Etten
R L
RL
Lawrence
C M
CM
Stauffacher
C V
CV
D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D017027:Protein Tyrosine Phosphatases