Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase.
(2002) Acta crystallographica. Section D, Biological crystallography — Vol. 58, n° Pt 1, p. 133-134 (2002)
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- Abstract
- 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.
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Citations
Peeraer, Y., Rabijns, A., Verboven, C., Collet, J.-F., Van Schaftingen, E., & De Ranter, C. (2002). Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase. Acta crystallographica. Section D, Biological crystallography, 58(Pt 1), 133-134. https://doi.org/10.1107/S0907444901017310 (Original work published 2002)