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.

Frq2 from drosophila melanogaster : Cloning, expression, purification, crystallization and preliminary X-ray analysis / S. Banos-Mateos, A. Chaves-Sanjuan, A. Mansilla, A. Ferrus, M.J. Sanchez-Barrena. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY COMMUNICATIONS. - ISSN 2053-230X. - F70:part 4(2014 Apr), pp. 530-534. [10.1107/S2053230X14005408]

Frq2 from drosophila melanogaster : Cloning, expression, purification, crystallization and preliminary X-ray analysis

A. Chaves-Sanjuan;
2014-04

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.
calcium-binding proteins; drosophila melanogaster; Frq2; animals; crystallization; crystallography, X-ray; drosophila proteins; cloning, molecular
Settore BIO/10 - Biochimica
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/902930
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