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Expression, purification, crystallization and preliminary X-ray diffraction analysis of human phosphoribosyl pyrophosphate synthetase 1 (PRS1). | LitMetric

Expression, purification, crystallization and preliminary X-ray diffraction analysis of human phosphoribosyl pyrophosphate synthetase 1 (PRS1).

Acta Crystallogr Sect F Struct Biol Cryst Commun

Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.

Published: May 2006

AI Article Synopsis

Article Abstract

Phosphoribosyl pyrophosphate synthetase (PRS; EC 2.7.6.1) catalyzes the reaction of ribose-5-phosphate (R5P) with ATP to yield AMP and PRPP (5-phosphoribosyl-1-pyrophosphate), which is necessary for the de novo and salvage pathways of purine-, pyrimidine- and pyridine-nucleotide biosynthesis. PRPP is a metabolite that is required at all times in the cell and is thus central to life. In this study, human PRS1 was produced in Escherichia coli in soluble form and purified to homogeneity. Crystals in complex with Mg2+, inorganic phosphate (P(i)) and ATP were obtained by the hanging-drop vapour-diffusion method. Diffraction data were collected to 2.6 A resolution. The crystal belongs to space group R3, with unit-cell parameters a = b = 168.846, c = 61.857 angstroms, assuming two molecules in the asymmetric unit and a volume-to-weight ratio of 2.4 angstroms3 Da(-1), which was consistent with the result calculated from the self-rotation function.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2219982PMC
http://dx.doi.org/10.1107/S1744309106009067DOI Listing

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