Crystallization of the major cytosolic glutathione S-transferase from Onchocerca volvulus.
Acta Crystallogr D Biol Crystallogr
; 60(Pt 8): 1496-7, 2004 Aug.
Article
in En
| MEDLINE
| ID: mdl-15272188
ABSTRACT
Glutathione S-transferases (GSTs) are a family of detoxification enzymes that catalyse the conjugation of glutathione to xenobiotic and endogenous electrophilic compounds, thus facilitating their elimination from cells. The recombinant Onchocerca volvulus GST2 has been expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion technique. Two different crystal forms were grown under identical conditions. They belong to space groups P2(1)2(1)2 and P2(1), respectively. The unit-cell parameters obtained are a = 112.6, b = 84.3, c = 45.1 A for the P2(1)2(1)2 crystal form and a = 51.6, b = 82.3, c = 56.7 A, beta = 95.89 degrees for the P2(1) form. Complete data sets to 2.6 and 1.5 A, respectively, have been collected at 100 K with synchrotron radiation.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Onchocerca volvulus
/
Cytosol
/
Glutathione Transferase
Limits:
Animals
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
2004
Document type:
Article
Affiliation country:
Alemania