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Updated: Aug 11, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
Published on: March 11, 2022
Crystallization and preliminary X-ray diffraction analysis of calexcitin from Loligo pealei: a neuronal protein
G D E Beaven1, P T Erskine, J N Wright
1School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, England.
Abstract:
The neuronal protein calexcitin from the long-finned squid Loligo pealei has been expressed in Escherichia coli and purified to homogeneity. Calexcitin is a 22 kDa calcium-binding protein that becomes up-regulated in invertebrates following Pavlovian conditioning and is likely to be involved in signal transduction events associated with learning and memory. Recombinant squid calexcitin has been crystallized using the hanging-drop vapour-diffusion technique in the orthorhombic space group P2(1)2(1)2(1). The unit-cell parameters of a = 46.6, b = 69.2, c = 134.8 A suggest that the crystals contain two monomers per asymmetric unit and have a solvent content of 49%. This crystal form diffracts X-rays to at least 1.8 A resolution and yields data of high quality using synchrotron radiation.

