Purification, crystallization and X-ray diffraction analysis of human synaptotagmin 1 C2A-C2B
- Department of Neuroscience and Cell Biology, The University of Texas Medical Branch, Galveston, TX 77555-0437 (United States)
- Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-0437 (United States)
- Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555-0437 (United States)
Human synaptotagmin C2A-C2B has been expressed as a glutathione-S-transferase fusion protein in Escherichia coli. The purification, crystallization and preliminary X-ray analysis of this protein are reported here. Synaptotagmin acts as the Ca{sup 2+} sensor for neuronal exocytosis. The cytosolic domain of human synaptotagmin 1 is composed of tandem C2 domains: C2A and C2B. These C2 domains modulate the interaction of synaptotagmin with the phospholipid bilayer of the presynaptic terminus and effector proteins such as the SNARE complex. Human synaptotagmin C2A-C2B has been expressed as a glutathione-S-transferase fusion protein in Escherichia coli. The purification, crystallization and preliminary X-ray analysis of this protein are reported here. The crystals diffract to 2.7 Å and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 82.37, b = 86.31, c = 140.2 Å. From self-rotation function analysis, there are two molecules in the asymmetric unit. The structure determination of the protein using this data is ongoing.
- OSTI ID:
- 22360157
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 9 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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