Literature DB >> 15103132

Crystals of the beta-subunit of bovine luteinizing hormone and indicators for the involvement of proteolysis in protein crystallization.

Alexander McPherson1, John Day, Lisa J Harris.   

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.

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Year:  2004        PMID: 15103132     DOI: 10.1107/S0907444904005025

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  3 in total

Review 1.  Optimization of crystallization conditions for biological macromolecules.

Authors:  Alexander McPherson; Bob Cudney
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-10-31       Impact factor: 1.056

2.  Four crystal forms of a Bence-Jones protein.

Authors:  Debora L Makino; Agnes H Henschen-Edman; Alexander McPherson
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2004-12-02

3.  Salvage and storage of infectious disease protein targets in the SSGCID high-throughput crystallization pathway using microfluidics.

Authors:  Jeff Christensen; Cory J Gerdts; Mathew C Clifton; Lance Stewart
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-08-13
  3 in total

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