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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 4(70), p. 530-534, 2014

DOI: 10.1107/s2053230x14005408

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Frq2 fromDrosophila melanogaster: cloning, expression, purification, crystallization and preliminary X-ray analysis

Journal article published in 2014 by Soledad Baños-Mateos, Antonio Chaves-Sanjuán ORCID, Alicia Mansilla, Alberto Ferrús, María José Sánchez-Barrena
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Drosophila melanogaster contains two calcium-binding proteins, Frq1 and Frq2, in the nervous system that control the number of synapses and the probability of release. To understand the differential function of the two proteins, whose sequence is only 5% dissimilar, the crystal structures of Frq1 and Frq2 are needed. Here, the cloning, expression, purification, crystallization and preliminary crystallographic analysis of Frq2 are presented. The full-length protein was purified using a two-step chromatographic procedure. Two different diffracting crystal forms were obtained using a progressive streak-seeding method and detergents.