Crystallization of recombinant Crithidia fasciculata tryparedoxin

Magnus S. Alphey; Emmanuel Tetaud; David G. Gourley; Alan H. Fairlamb; William N. Hunter

doi:10.1006/jsbi.1999.4091

Crystallization of recombinant Crithidia fasciculata tryparedoxin

Magnus S. Alphey
, Emmanuel Tetaud
, David G. Gourley
, Alan H. Fairlamb
, William N. Hunter (Lead / Corresponding author)

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

6 Citations (Scopus)

Abstract

Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P2₁2₁2₁, with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 Å, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Å resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.

Original language	English
Pages (from-to)	76-79
Number of pages	4
Journal	Journal of Structural Biology
Volume	126
Issue number	1
DOIs	https://doi.org/10.1006/jsbi.1999.4091
Publication status	Published - 1 Jun 1999

Keywords

Crithidia fasciculata
Crystallization
Thioredoxin
Tryparedoxin
X-ray diffraction

ASJC Scopus subject areas

Structural Biology

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10.1006/jsbi.1999.4091

Cite this

@article{d82c64b345834ac0a0c49f3344e053c4,

title = "Crystallization of recombinant Crithidia fasciculata tryparedoxin",

abstract = "Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 {\AA}, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-{\AA} resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.",

keywords = "Crithidia fasciculata, Crystallization, Thioredoxin, Tryparedoxin, X-ray diffraction",

author = "Alphey, \{Magnus S.\} and Emmanuel Tetaud and Gourley, \{David G.\} and Fairlamb, \{Alan H.\} and Hunter, \{William N.\}",

note = "Funding Information: This research is supported by the BBSRC, The Wellcome Trust, CCLRC, and the University of Dundee. We are grateful to Dr. A.",

year = "1999",

month = jun,

day = "1",

doi = "10.1006/jsbi.1999.4091",

language = "English",

volume = "126",

pages = "76--79",

journal = "Journal of Structural Biology",

issn = "1047-8477",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Crystallization of recombinant Crithidia fasciculata tryparedoxin

AU - Alphey, Magnus S.

AU - Tetaud, Emmanuel

AU - Gourley, David G.

AU - Fairlamb, Alan H.

AU - Hunter, William N.

N1 - Funding Information: This research is supported by the BBSRC, The Wellcome Trust, CCLRC, and the University of Dundee. We are grateful to Dr. A.

PY - 1999/6/1

Y1 - 1999/6/1

N2 - Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 Å, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Å resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.

AB - Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 Å, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Å resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.

KW - Crithidia fasciculata

KW - Crystallization

KW - Thioredoxin

KW - Tryparedoxin

KW - X-ray diffraction

UR - https://www.scopus.com/pages/publications/0033150407

U2 - 10.1006/jsbi.1999.4091

DO - 10.1006/jsbi.1999.4091

M3 - Article

C2 - 10329491

AN - SCOPUS:0033150407

SN - 1047-8477

VL - 126

SP - 76

EP - 79

JO - Journal of Structural Biology

JF - Journal of Structural Biology

IS - 1

ER -

Crystallization of recombinant Crithidia fasciculata tryparedoxin

Abstract

Keywords

ASJC Scopus subject areas

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