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

doi:10.1006/jmbi.1993.1475

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

Biological Chemistry and Drug Discovery

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	1217-1220
Number of pages	4
Journal	Journal of Molecular Biology
Volume	232
Issue number	4
DOIs	https://doi.org/10.1006/jmbi.1993.1475
Publication status	Published - 20 Aug 1993

Keywords

Molecular replacement
Protein crystallization
Trypanothione reductase
X-ray diffraction

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1006/jmbi.1993.1475

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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 = aug,

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",

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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

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AN - SCOPUS:0027197376

SN - 0022-2836

VL - 232

SP - 1217

EP - 1220

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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