These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Crystals of the beta-subunit of bovine luteinizing hormone and indicators for the involvement of proteolysis in protein crystallization.
    Author: McPherson A, Day J, Harris LJ.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 May; 60(Pt 5):872-7. PubMed ID: 15103132.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]