Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 12 (December 2005)

crystallization communications

Acta Cryst. (2005). F61, 1058-1061 [ doi:10.1107/S1744309105035384 ]

Improved expression, purification and crystallization of a putative N-acetyl--glutamyl-phosphate reductase from rice (Oryza sativa)

J. Miura-Ohnuma, T. Nonaka, S. Katoh, K. Murata, A. Kita, K. Miki and E. Katoh

Abstract: N-Acetyl- [gamma] -glutamyl-phosphate reductase (AGPR) catalyzes the third step in an eight-step arginine-biosynthetic pathway that starts with glutamate. This enzyme converts N-acetyl- [gamma] -glutamyl phosphate to N-acetylglutamate- [gamma] -semialdehyde by an NADPH-dependent reductive dephosphorylation. AGPR from Oryza sativa (OsAGPR) was expressed in Escherichia coli at 291 K as a soluble fusion protein with an upstream thioredoxin-hexahistidine [Trx-(His)₆] extension. OsAGPR(Ala50-Pro366) was purified and crystals were obtained using the sitting-drop vapour-diffusion method at 293 K and diffract X-rays to at least 1.8 Å resolution. They belong to the hexagonal space group P6₁, with unit-cell parameters a = 86.11, c = 316.3 Å.

Keywords: rice (Oryza sativa); N-acetyl--glutamyl-phosphate reductase (AGPR).


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