Expression, purification and preliminary X-ray characterization of N-acetyl-γ-glutamyl-phosphate reductase from Thermus thermophilus HB8
Acta Crystallographica Section D
Volume 59, Issue 2, pages 356–358, February 2003
How to Cite
Goto, M., Agari, Y., Omi, R., Miyahara, I. and Hirotsu, K. (2003), Expression, purification and preliminary X-ray characterization of N-acetyl-γ-glutamyl-phosphate reductase from Thermus thermophilus HB8. Acta Cryst. D, 59: 356–358. doi: 10.1107/S0907444902020802
- N-acetyl-γ-glutamyl-phosphate reductase.
N-Acetyl-γ-glutamyl-phosphate reductase (AGPR) catalyses the NADPH-dependent reduction of N-acetyl-γ-glutamyl phosphate to give the N-acetylglutamic semialdehyde. A recombinant form of AGPR from Thermus thermophilus HB8 has been crystallized by the hanging-drop vapour-diffusion technique using PEG 4000 as a precipitating agent. The crystals grew as colourless prisms, with unit-cell parameters a = b = 90.9, c = 139.5 Å, α = β = 90, γ = 120°. The crystals belong to the hexagonal space group P6222 or P6422 and are most likely to contain a monomer in the asymmetric unit, with a VM value of 2.19 Å3 Da−1. The crystals diffract to a resolution of 2.2 Å at beamline BL44B2 of SPring-8.