Crystallization and preliminary X-ray diffraction analysis of calexcitin from Loligo pealei: a neuronal protein implicated in learning and memory
Beaven, G.D.E., Erskine, P.T., Wright, J.N., Mohammed, F., Gill, R.., Wood, S., Vernon, J., Giese, K.P. and Copper, J.B. (2005) Crystallization and preliminary X-ray diffraction analysis of calexcitin from Loligo pealei: a neuronal protein implicated in learning and memory. Acta Crystallographica, Section F - Structural Biology And Crystallization Communications, 61, (10), 879-881. (doi:10.1107/S1744309105026758). (Submitted).
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Description/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 P212121. The unit-cell parameters of a = 46.6, b = 69.2, c = 134.8 Å 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 Å resolution and yields data of high quality using synchrotron radiation.
| Item Type: | Article |
|---|---|
| ISSNs: | 1744-3091 (print) |
| Related URLs: | |
| Keywords: | calexcitin, calcium-binding proteins |
| Subjects: | Q Science > QH Natural history > QH301 Biology |
| Divisions: | University Structure - Pre August 2011 > School of Biological Sciences |
| Item ID: | 35627 |
| Date Deposited: | 22 May 2006 |
| Last Modified: | 28 Jun 2012 10:22 |
| Contributors: | Beaven, G.D.E. (Author) Erskine, P.T. (Author) Wright, J.N. (Author) Mohammed, F. (Author) Gill, R.. (Author) Wood, S. (Author) Vernon, J. (Author) Giese, K.P. (Author) Copper, J.B. (Author) |
| Date: | 13 September 2005 |
| Status: | Submitted |
| Contact Email Address: | j.b.copper@soton.ac.uk |
| URI: | http://eprints.soton.ac.uk/id/eprint/35627 |
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