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

ABSTRACT: Protein tyrosine phosphatase ? is a membrane-bound receptor and is designated RPTP?. RPTP? and two mutants, RPTP?(V948I, S970T) and RPTP?(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.

SUBMITTER: Kish K 

PROVIDER: S-EPMC3144792 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature