Volume 70, Issue 11 pp. 1536-1539

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the extracellular olfactomedin domain of gliomedin

First published: 05 November 2014
Huijong Han, e-mail: [email protected]; Petri Kursula, e-mail: [email protected]

Abstract

Gliomedin (GLDN) is one of the essential proteins in the development of the nodes of Ranvier in the vertebrate peripheral nervous system. An olfactomedin (OLF) domain is located at the GLDN extracellular C-terminus and is involved in the accumulation of neuronal plasma membrane voltage-gated sodium channels in the nodes by interacting with neurofascin and NrCAM. No structures of OLF domains have previously been reported. Here, the crystallization of the rat GLDN OLF domain, which was expressed in an insect-cell system, is reported. The crystal diffracted to 1.55 Å resolution and belonged to space group P21, with unit-cell parameters a = 37.5, b = 141.7, c = 46.0 Å, β = 110.6°, and had two molecules in the asymmetric unit.

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