Expression, purification and preliminary crystallographic analysis of sucrose phosphate synthase (SPS) from Halothermothrix orenii.
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 A, beta = 103.16 degrees, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 3.01 A. Heavy-metal and halide-soaking trials are currently in progress to solve the structure.
Huynh
Frederick
F
Microbial Gene Research and Resources Facility, School of Biomolecular and Biomedical Sciences, Faculty of Science, Griffith University, Brisbane, Queensland 4111, Australia.
Tan
Tien-Chye
TC
Swaminathan
Kunchithapadam
K
Patel
Bharat K C
BK
D001419:Bacteria / Q000201:enzymology*; D003460:Crystallization; D005964:Glucosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D015183:Restriction Mapping; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D005964:Glucosyltransferases; C022698:sucrose-phosphate synthase