Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase

This is the authors' abstract. We don't add key points for this paper.

Phosphoserine phosphatase (PSP), a human enzyme involved in the L-serine biosynthesis pathway, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03 A, b = 130.25 A, c = 157.29 A. Calculation of the Matthews coefficient indicates that there are two molecules in the asymmetric unit. A complete native data set to a resolution of 1.53 A has been collected at 100 K using synchrotron radiation.