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Updated: May 1, 2026

Purification of Transcripts and Metabolites from Drosophila Heads
Published on: March 15, 2013
Frq2 from Drosophila melanogaster: cloning, expression, purification, crystallization and preliminary X-ray analysis
Soledad Baños-Mateos1, Antonio Chaves-Sanjuán1, Alicia Mansilla2
1Department of Crystallography and Structural Biology, Institute of Physical Chemistry `Rocasolano', CSIC, Serrano 119, 28006 Madrid, Spain.
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.

