Literature DB >> 7932760

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

M Tegoni1, M C Silvestrini, V S Lamzin, M Brunori, C 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).

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Year:  1994        PMID: 7932760     DOI: 10.1006/jmbi.1994.1659

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties.

Authors:  F Cutruzzola; K Brown; E K Wilson; A Bellelli; M Arese; M Tegoni; C Cambillau; M Brunori
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-27       Impact factor: 11.205

2.  Structure of heme d1-free cd1 nitrite reductase NirS.

Authors:  Thomas Klünemann; Wulf Blankenfeldt
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2020-05-29       Impact factor: 1.056

  2 in total

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