Crystals of the beta-subunit of bovine luteinizing hormone and indicators for the involvement of proteolysis in protein crystallization.
The beta-subunit of luteinizing hormone (LH), the subunit responsible for the physiological response, has been crystallized beginning with the intact alphabeta-heterodimeric hormone purified from bovine pituitary glands. The crystals were grown at 310 K in the presence of neutral detergents along with trypsin. The tetragonal bipyramidal crystals diffract to 3 A resolution and belong to space group I4(1)22, with unit-cell parameters a = b = 57, c = 207 A. It is noted that proteins exposed to proteases sometimes yield products that crystallize better than the native molecule and that the beta-subunit of LH represents yet another example. Some indicators of when proteolysis may be a factor in crystallization, as well as some consequences, are described.
McPherson
Alexander
A
Department of Molecular Biology and Biochemistry, 560 Steinhaus Hall, Irvine, CA 92697-3900, USA. amcphers@uci.edu
Day
John
J
Harris
Lisa J
LJ
D000818:Animals; D001671:Biochemistry / Q000379:methods; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D037101:Luteinizing Hormone, beta Subunit / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D010902:Pituitary Gland / Q000737:chemistry; D011487:Protein Conformation; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism
D037101:Luteinizing Hormone, beta Subunit; D010447:Peptide Hydrolases; D014357:Trypsin