Alain Roussel
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Alain Roussel has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
Christine Kellenberger
2 shared publications- Franck Coste
Centre de Biophysique Moléculaire, UPR4301 CNRS, 45071 Orléans Cedex 2, France
2 shared publications Yumiko Mishima
Centre de Biophysique Moléculaire, UPR 4301 CNRS, 45071 Orléans Cedex 2, France
2 shared publicationsCecile Clavaud
1 shared publicationCharles Hetru
1 shared publication- Dominique Ferrandon
Institut de Biologie Moléculaire et Cellulaire
1 shared publication
Latest Publications
- Open Access
- 1 October 2009
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (42) , 28687-28697
The N-terminal Domain of Drosophila Gram-negative Binding Protein 3 (GNBP3) Defines a Novel Family of Fungal Pattern Recognition Receptors
- 1 October 2009
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (42) , 28687-28697
Open AccessThe N-terminal Domain of Drosophila Gram-negative Binding Protein 3 (GNBP3) Defines a Novel Family of Fungal Pattern Recognition Receptors
- 20 August 2009
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 65 (9) , 870-873
Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 fromDrosophila melanogaster
Gram-negative bacteria-binding protein 3 (GNBP3) is a pattern-recognition receptor which contributes to the defensive response against fungal infection in Drosophila. The protein consists of an N-terminal domain, which is considered to recognize -glucans from the fungal cell wall, and a C-terminal domain, which is homologous to bacterial glucanases but devoid of activity. The N-terminal domain of GNBP3 (GNBP3-Nter) was successfully purified after expression in Drosophila S2 cells. Diffraction-quality crystals were produced by the hanging-drop vapour-diffusion method using PEG 2000 and PEG 8000 as precipitants. Preliminary X-ray diffraction analysis revealed that the GNBP3-Nter crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 134.79, b = 30.55, c = 51.73 Å, = 107.4°, and diffracted to 1.7 Å using synchrotron radiation. The asymmetric unit is expected to contain two copies of GNBP3-Nter. Heavy-atom derivative data were collected and a samarium derivative showed one high-occupancy site per molecule.
- 20 August 2009
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 65 (9) , 870-873
Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 fromDrosophila melanogaster
Gram-negative bacteria-binding protein 3 (GNBP3) is a pattern-recognition receptor which contributes to the defensive response against fungal infection in Drosophila. The protein consists of an N-terminal domain, which is considered to recognize -glucans from the fungal cell wall, and a C-terminal domain, which is homologous to bacterial glucanases but devoid of activity. The N-terminal domain of GNBP3 (GNBP3-Nter) was successfully purified after expression in Drosophila S2 cells. Diffraction-quality crystals were produced by the hanging-drop vapour-diffusion method using PEG 2000 and PEG 8000 as precipitants. Preliminary X-ray diffraction analysis revealed that the GNBP3-Nter crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 134.79, b = 30.55, c = 51.73 Å, = 107.4°, and diffracted to 1.7 Å using synchrotron radiation. The asymmetric unit is expected to contain two copies of GNBP3-Nter. Heavy-atom derivative data were collected and a samarium derivative showed one high-occupancy site per molecule.