Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 from Drosophila melanogaster - Archive ouverte HAL Access content directly
Journal Articles Acta crystallographica Section F : Structural biology communications [2014-...] Year : 2009

Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 from Drosophila melanogaster

Abstract

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 beta-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 angstrom, beta = 107.4 degrees, and diffracted to 1.7 angstrom 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.

Dates and versions

hal-00525123 , version 1 (11-10-2010)

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Yumiko Mishima, Franck Coste, Vanessa Bobezeau, Nadège Hervouet, Christine Kellenberger, et al.. Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 from Drosophila melanogaster. Acta crystallographica Section F : Structural biology communications [2014-..], 2009, 65 (Part 9), pp.870-873. ⟨10.1107/S1744309109014997⟩. ⟨hal-00525123⟩
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