Pravien D Abeywickrema,
Sangita B Patel,
Noel J Byrne,
Ronald E Diehl,
Dawn L Hall,
Rachael E Ford,
Keith W Rickert,
John C Reid,
Jennifer M Shipman,
Wayne M Geissler, Kelly D Pryor,
Ranabir SinhaRoy,
Stephen M Soisson,
Kevin J Lumb,
Sujata Sharma
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ABSTRACT: Prolylcarboxypeptidase (PrCP) is a lysosomal serine carboxypeptidase that cleaves a variety of C-terminal amino acids adjacent to proline and has been implicated in diseases such as hypertension and obesity. Here, the robust production, purification and crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yielded crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffracted to better than 2.8 A resolution.
Acta Crystallographica Section F Structural Biology and Crystallization Communications 06/2010; 66(Pt 6):702-5. · 0.51 Impact Factor
