Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae

P. H. Roberts; X. Zhou; A. M. Holmes; Hilary Ranson; Graham Small; Janet Hemingway; J. D. Ng; L. Chen; E. J. Meehan

doi:10.1107/s0907444900013810

Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae

P. H. Roberts
, X. Zhou
, A. M. Holmes
, Hilary Ranson
, Graham Small
, Janet Hemingway
, J. D. Ng
, L. Chen
, E. J. Meehan

University of Alabama in Huntsville

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

5 Citations (Scopus)

Abstract

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 Å 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 Å. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.

Original language	English
Pages (from-to)	134-136
Number of pages	3
Journal	Acta Crystallographica Section D: Structural Biology
Volume	57
Issue number	1
DOIs	https://doi.org/10.1107/s0907444900013810
Publication status	Published - 1 Jan 2001
Externally published	Yes

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title = "Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae",

abstract = "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 {\AA} 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 {\AA}. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.",

author = "Roberts, \{P. H.\} and X. Zhou and Holmes, \{A. M.\} and Hilary Ranson and Graham Small and Janet Hemingway and Ng, \{J. D.\} and L. Chen and Meehan, \{E. J.\}",

year = "2001",

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doi = "10.1107/s0907444900013810",

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T1 - Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae

AU - Roberts, P. H.

AU - Zhou, X.

AU - Holmes, A. M.

AU - Ranson, Hilary

AU - Small, Graham

AU - Hemingway, Janet

AU - Ng, J. D.

AU - Chen, L.

AU - Meehan, E. J.

PY - 2001/1/1

Y1 - 2001/1/1

N2 - 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 Å 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 Å. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.

AB - 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 Å 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 Å. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.

U2 - 10.1107/s0907444900013810

DO - 10.1107/s0907444900013810

M3 - Article

SN - 1399-0047

VL - 57

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EP - 136

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

IS - 1

ER -

Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae

Abstract

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