Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase.
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.
Peeraer
Yves
Y
Laboratory for Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium.
Rabijns
Anja
A
Verboven
Christel
C
Collet
Jean François
JF
Van Schaftingen
Emile
E
De Ranter
Camiel
C
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
D010744:Phosphoric Monoester Hydrolases; C022394:phosphoserine phosphatase