Cloning, purification, crystallization and preliminary X-ray analysis of the catalytic domain of human receptor-like protein tyrosine phosphatase γ in three different crystal forms.

Kevin Kish, Patricia A McDonnell, Valentina Goldfarb, Mian Gao, William J Metzler, David R Langley, James W Bryson, Susan E Kiefer, Brian Carpenter, Walter A Kostich, Ryan S Westphal, Steven Sheriff

Bristol-Myers Squibb Research and Development, Princeton, NJ 08543-4000, USA.

Acta crystallographica. Section F, Structural biology and crystallization communications 2011 Jul 1

filter terms:

Protein tyrosine phosphatase γ is a membrane-bound receptor and is designated RPTPγ. RPTPγ and two mutants, RPTPγ(V948I, S970T) and RPTPγ(C858S, S970T), were recombinantly expressed and purified for X-ray crystallographic studies. The purified enzymes were crystallized using the hanging-drop vapor-diffusion method. Crystallographic data were obtained from several different crystal forms in the absence and the presence of inhibitor. In this paper, a description is given of how three different crystal forms were obtained that were used with various ligands. An orthorhombic crystal form and a trigonal crystal form were obtained both with and without ligand, and a monoclinic crystal form was only obtained in the presence of a particularly elaborated inhibitor.

Citation

Kevin Kish, Patricia A McDonnell, Valentina Goldfarb, Mian Gao, William J Metzler, David R Langley, James W Bryson, Susan E Kiefer, Brian Carpenter, Walter A Kostich, Ryan S Westphal, Steven Sheriff. Cloning, purification, crystallization and preliminary X-ray analysis of the catalytic domain of human receptor-like protein tyrosine phosphatase γ in three different crystal forms. Acta crystallographica. Section F, Structural biology and crystallization communications. 2011 Jul 1;67(Pt 7):768-74