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. 2004 Dec;60(Pt 12 Pt 2):2364-7.
doi: 10.1107/S0907444904026861. Epub 2004 Nov 26.

Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

Fabien Bonneau  1 , Igor D'Angelo, Stefan Welti, Gunter Stier, Jari Ylänne, Klaus Scheffzek
Affiliations

Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

Fabien Bonneau et al. Acta Crystallogr D Biol Crystallogr. 2004 Dec.

Abstract

Neurofibromin (MW 320 kDa) is the protein responsible for the pathogenesis of neurofibromatosis type 1 (NF1), one of the most common genetic diseases worldwide. The neurofibromin GAP-related domain (GRD, MW 38 kDa) possess a Ras-specific GTPase-activating protein property, which is at present its only clear biochemical function. This article describes the study of the bacterial production and preliminary X-ray crystallographic analysis of a neurofibromin fragment located at the C-terminal end of the GRD, which contains a region reported to be homologous to the yeast Sec14p lipid exchange protein. Of the three crystal variants obtained, a tetragonal form diffracted to a resolution of at least 2.3 A.

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