Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae.
Glutathione S-transferases (GSTs) belong to a family of detoxification enzymes that conjugate glutathione to various xenobiotics, thus facilitating their expulsion from the cell. GST activity is elevated in many insecticide-resistant insects, including the DDT-resistant malaria vector Anopheles gambiae. Crystals of the recombinant form of a GST from A. gambiae, agGST1-6, have been grown in at least five different crystal forms, with a broad range of diffraction resolution limits. A complete 2.0 A data set has been collected on a C-centered orthorhombic crystal form with unit-cell parameters a = 99.0, b = 199.4, c = 89.6 A. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.
Roberts
P H
PH
Laboratory for Structural Biology, University of Alabama in Huntsville, MSB 203C, Huntsville, AL 35899, USA.
Zhou
X
X
Holmes
A M
AM
Ranson
H
H
Small
G
G
Hemingway
J
J
Ng
J D
JD
Chen
L
L
Meehan
E J
EJ
D000818:Animals; D000852:Anopheles / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003634:DDT; D005982:Glutathione Transferase / Q000737:chemistry*; D007305:Insecticide Resistance; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D003634:DDT; D005982:Glutathione Transferase