Crystallization and preliminary X-ray analysis of a new crystal form of nitrite reductase from Pseudomonas aeruginosa

Journal of Molecular Biology
M TegoniC Cambillau

Abstract

Nitrite reductase from Pseudomonas aeruginosa (EC 1.9.3.2), a redox enzyme synthesized by the bacterium grown in the presence of nitrate, is a soluble dimer of two identical subunits of 60 kDa, each containing one c and one d1 haem as prosthetic groups. A new crystal from of the Ps. aeruginosa nitrite reductase in the oxidized state, suitable for X-ray structure determination, has been obtained by vapour diffusion at 20 degrees C, in the presence of 10% polyethylene glycol 4000, 50 mM Tris-HCl (pH 8.7), 400 mM NaCl and at a protein concentration of 14 mg/ml. The crystals are dark green elongated tetragonal prisms of dimensions 1.5 mm x 0.2 mm x 0.2 mm for the largest ones. These crystals are tetragonal with space group P4(1(3))2(1)2 and cell dimensions a = b = 128.2 A, c = 172.6 A. They diffract at least up to 2.8 A. Assuming a dimer in the asymmetric unit, the VM value is 2.95 A3/Da (58% of solvent).

Citations

Feb 28, 2001·Proceedings of the National Academy of Sciences of the United States of America·F CutruzzolaM Brunori
Jun 9, 2020·Acta Crystallographica. Section F, Structural Biology Communications·Thomas Klünemann, Wulf Blankenfeldt
Sep 21, 2001·Journal of Molecular Biology·K BrownM Tegoni

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