Expression, purification and preliminary crystallographic analysis of sucrose phosphate synthase (SPS) from Halothermothrix orenii. .
Author(s)
Huynh, Frederick
Tan, Tien-Chye
Swaminathan, Kunchithapadam
Patel, Bharat KC
Year published
2005
Metadata
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This is the first report of the crystallization of a sucrose phosphate synthase (SPS; EC 2.4.1.14). It also constitutes the first study of a sucrose phosphate synthase from a non-photosynthetic thermohalophilic anaerobic bacterium, Halothermothrix orenii. The purified recombinant spsA protein has been crystallized in the monoclinic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 72.3 Ŭ = 103.16ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 3.01 Ů Heavy-metal and halide-soaking trials are currently in progress to solve the structure.This is the first report of the crystallization of a sucrose phosphate synthase (SPS; EC 2.4.1.14). It also constitutes the first study of a sucrose phosphate synthase from a non-photosynthetic thermohalophilic anaerobic bacterium, Halothermothrix orenii. The purified recombinant spsA protein has been crystallized in the monoclinic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 72.3 Ŭ = 103.16ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 3.01 Ů Heavy-metal and halide-soaking trials are currently in progress to solve the structure.
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Journal Title
Acta Crystallograph Section F Structrural Biology and Crystallization Communications
Volume
F61
Subject
Chemical Sciences
Biological Sciences