Crystallization and preliminary x-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2.

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Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 2008 Jul 1;64:629-31. doi: 10.1107/S1744309108016059

Crystallization and preliminary x-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2. Looger LabSchreiter Lab

Guilbe MM, Malavé EC, Akerboom J, Marvin JS, Looger LL, Schreiter ER

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Abstract

Fluorescent proteins and their engineered variants have played an important role in the study of biology. The genetically encoded calcium-indicator protein GCaMP2 comprises a circularly permuted fluorescent protein coupled to the calcium-binding protein calmodulin and a calmodulin target peptide, M13, derived from the intracellular calmodulin target myosin light-chain kinase and has been used to image calcium transients in vivo. To aid rational efforts to engineer improved variants of GCaMP2, this protein was crystallized in the calcium-saturated form. X-ray diffraction data were collected to 2.0 A resolution. The crystals belong to space group C2, with unit-cell parameters a = 126.1.

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Crystallization and preliminary x-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2.

Abstract