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Crystallization (Commentary)
2.3 A resolution crystal structure of apoenzyme using Hg-multiwavelength anomalous dispersion phasing, vapor diffusion method, crystals belong to space group P2(1)2(1)2(1), in which each bifunctional monomer contains a dethiobiotin synthetase-like amidoligase N-terminal domain and a type 1 glutamine amidotransferase C-terminal domain
crystal structure analysis discloses a homotetrameric structure and each active site is formed by three different subunits. Sulfate ions bound to the active sites indicate the positions of phosphate-binding sites for the substrates ATP and UTP and the feedback inhibitor CTP. Together with earlier structures of bacterial CTPS, the human CTPS structure provides an extended understanding of the structure–function relationship of CTPS-family members; the protein is crystallized by the hanging-drop method, equilibrating 1 ml protein solution and 1 ml of a solution containing 0.1 M Tris pH 8.8, 1.2 M (NH4)2SO4 and 50 mM malonic acid against 0.5 ml of a well solution containing 0.1 M Tris pH 8.8 and 1.2 M (NH4)2SO4. Crystals with a maximum dimension of 0.03 nm formed in 3 d
crystal structures of Thermus thermophilus HB8 CTP synthetase as a tetramer in its native form, CTP synthetase as complex with 3 SO42- and CTP synthetase as a complex with glutamine. Crystallization at 20 °C using vapor-diffusion method. The space group is I222 with cell dimensions of a = 90.4 A, b = 117.1 A and c = 142.3 A
dimeric form of CTP synthase at 2.5 A resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of Sulfolobus solfataricus CTP synthase all have large thermal parameters in the dimeric form and undergo substantial movement upon tetramerization
hanging-drop vapour-diffusion technique
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