Literature DB >> 2254926

Initiating a crystallographic study of trypanothione reductase.

W N Hunter1, K Smith, Z Derewenda, S J Harrop, J Habash, M S Islam, J R Helliwell, A H Fairlamb.   

Abstract

We have obtained well-ordered single crystals of the flavoenzyme trypanothione reductase from Crithidia fasciculata. The crystals are tetragonal rods with unit cell dimensions a = 128.6 A, c = 92.5 A. The diffraction pattern corresponds to a primitive lattice. Laue class 4/m. Diffraction to better than 2.4 A has been recorded at the Daresbury Synchrotron. The accurate elucidation of the three-dimensional structure of this enzyme is required to support the rational design of compounds active against a variety of tropical diseases caused by trypanosomal parasites.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2254926     DOI: 10.1016/S0022-2836(05)80314-6

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


  2 in total

1.  X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution.

Authors:  J Kuriyan; X P Kong; T S Krishna; R M Sweet; N J Murgolo; H Field; A Cerami; G B Henderson
Journal:  Proc Natl Acad Sci U S A       Date:  1991-10-01       Impact factor: 11.205

2.  The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution.

Authors:  Y Zhang; C S Bond; S Bailey; M L Cunningham; A H Fairlamb; W N Hunter
Journal:  Protein Sci       Date:  1996-01       Impact factor: 6.725

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.