Trypanosoma cruzi trypanothione reductase: Crystallization, unit cell dimensions and structure solution

Yihong Zhang, Susan Bailey, James H. Naismith, Charles S. Bond, Jarjis Habash, Paul McLaughlin, Miroslav Z. Papiz, Adolfo Borges, Mark Cunningham, Alan H. Fairlamb, William N. Hunter

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

We have reproducibly crystallized recombinant trypanothione reductase from Trypanosoma cruzi. Yellow tetragonal crystals in the shape of elongated prisms have unit cell dimensions of a=92.8 Å, c=156.6 Å. Laue symmetry of 4/m and are suitable for a detailed structural analysis. Diffraction data to 2.7 Å resolution have been recorded using synchrotron radiation at the Daresbury laboratory. The structure has been solved by molecular replacement calculations using this synchrotron data and our previously determined Crithidia fasciculata enzyme structure as a search model. The space group has been identified as P43 with a homodimer of approximate molecular mass of 108 kDa in the asymmetric unit. Diffraction beyond 2.5 Å has been recorded when large freshly grown crystals are exposed to X-rays. Refinement of the structure is in progress.

Original languageEnglish
Pages (from-to)1217-1220
Number of pages4
JournalJournal of Molecular Biology
Volume232
Issue number4
DOIs
Publication statusPublished - 20 Aug 1993

Fingerprint

Synchrotrons
Trypanosoma cruzi
Crystallization
Crithidia fasciculata
X-Rays
Radiation
Enzymes
trypanothione reductase

Keywords

  • Molecular replacement
  • Protein crystallization
  • Trypanothione reductase
  • X-ray diffraction

Cite this

Zhang, Yihong ; Bailey, Susan ; Naismith, James H. ; Bond, Charles S. ; Habash, Jarjis ; McLaughlin, Paul ; Papiz, Miroslav Z. ; Borges, Adolfo ; Cunningham, Mark ; Fairlamb, Alan H. ; Hunter, William N. / Trypanosoma cruzi trypanothione reductase : Crystallization, unit cell dimensions and structure solution. In: Journal of Molecular Biology. 1993 ; Vol. 232, No. 4. pp. 1217-1220.
@article{d01ba391e9a04e4e869b0228e7b36060,
title = "Trypanosoma cruzi trypanothione reductase: Crystallization, unit cell dimensions and structure solution",
abstract = "We have reproducibly crystallized recombinant trypanothione reductase from Trypanosoma cruzi. Yellow tetragonal crystals in the shape of elongated prisms have unit cell dimensions of a=92.8 {\AA}, c=156.6 {\AA}. Laue symmetry of 4/m and are suitable for a detailed structural analysis. Diffraction data to 2.7 {\AA} resolution have been recorded using synchrotron radiation at the Daresbury laboratory. The structure has been solved by molecular replacement calculations using this synchrotron data and our previously determined Crithidia fasciculata enzyme structure as a search model. The space group has been identified as P43 with a homodimer of approximate molecular mass of 108 kDa in the asymmetric unit. Diffraction beyond 2.5 {\AA} has been recorded when large freshly grown crystals are exposed to X-rays. Refinement of the structure is in progress.",
keywords = "Molecular replacement, Protein crystallization, Trypanothione reductase, X-ray diffraction",
author = "Yihong Zhang and Susan Bailey and Naismith, {James H.} and Bond, {Charles S.} and Jarjis Habash and Paul McLaughlin and Papiz, {Miroslav Z.} and Adolfo Borges and Mark Cunningham and Fairlamb, {Alan H.} and Hunter, {William N.}",
year = "1993",
month = "8",
day = "20",
doi = "10.1006/jmbi.1993.1475",
language = "English",
volume = "232",
pages = "1217--1220",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Elsevier",
number = "4",

}

Zhang, Y, Bailey, S, Naismith, JH, Bond, CS, Habash, J, McLaughlin, P, Papiz, MZ, Borges, A, Cunningham, M, Fairlamb, AH & Hunter, WN 1993, 'Trypanosoma cruzi trypanothione reductase: Crystallization, unit cell dimensions and structure solution', Journal of Molecular Biology, vol. 232, no. 4, pp. 1217-1220. https://doi.org/10.1006/jmbi.1993.1475

Trypanosoma cruzi trypanothione reductase : Crystallization, unit cell dimensions and structure solution. / Zhang, Yihong; Bailey, Susan; Naismith, James H.; Bond, Charles S.; Habash, Jarjis; McLaughlin, Paul; Papiz, Miroslav Z.; Borges, Adolfo; Cunningham, Mark; Fairlamb, Alan H.; Hunter, William N.

In: Journal of Molecular Biology, Vol. 232, No. 4, 20.08.1993, p. 1217-1220.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Trypanosoma cruzi trypanothione reductase

T2 - Crystallization, unit cell dimensions and structure solution

AU - Zhang, Yihong

AU - Bailey, Susan

AU - Naismith, James H.

AU - Bond, Charles S.

AU - Habash, Jarjis

AU - McLaughlin, Paul

AU - Papiz, Miroslav Z.

AU - Borges, Adolfo

AU - Cunningham, Mark

AU - Fairlamb, Alan H.

AU - Hunter, William N.

PY - 1993/8/20

Y1 - 1993/8/20

N2 - We have reproducibly crystallized recombinant trypanothione reductase from Trypanosoma cruzi. Yellow tetragonal crystals in the shape of elongated prisms have unit cell dimensions of a=92.8 Å, c=156.6 Å. Laue symmetry of 4/m and are suitable for a detailed structural analysis. Diffraction data to 2.7 Å resolution have been recorded using synchrotron radiation at the Daresbury laboratory. The structure has been solved by molecular replacement calculations using this synchrotron data and our previously determined Crithidia fasciculata enzyme structure as a search model. The space group has been identified as P43 with a homodimer of approximate molecular mass of 108 kDa in the asymmetric unit. Diffraction beyond 2.5 Å has been recorded when large freshly grown crystals are exposed to X-rays. Refinement of the structure is in progress.

AB - We have reproducibly crystallized recombinant trypanothione reductase from Trypanosoma cruzi. Yellow tetragonal crystals in the shape of elongated prisms have unit cell dimensions of a=92.8 Å, c=156.6 Å. Laue symmetry of 4/m and are suitable for a detailed structural analysis. Diffraction data to 2.7 Å resolution have been recorded using synchrotron radiation at the Daresbury laboratory. The structure has been solved by molecular replacement calculations using this synchrotron data and our previously determined Crithidia fasciculata enzyme structure as a search model. The space group has been identified as P43 with a homodimer of approximate molecular mass of 108 kDa in the asymmetric unit. Diffraction beyond 2.5 Å has been recorded when large freshly grown crystals are exposed to X-rays. Refinement of the structure is in progress.

KW - Molecular replacement

KW - Protein crystallization

KW - Trypanothione reductase

KW - X-ray diffraction

UR - http://www.scopus.com/inward/record.url?scp=0027197376&partnerID=8YFLogxK

U2 - 10.1006/jmbi.1993.1475

DO - 10.1006/jmbi.1993.1475

M3 - Article

C2 - 8371273

AN - SCOPUS:0027197376

VL - 232

SP - 1217

EP - 1220

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 4

ER -