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Title: Crystallization and preliminary X-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2

Journal Article · · Acta Crystallographica. Section F
 [1];  [2]; ; ;  [3]
  1. Department of Biochemistry, University of Puerto Rico, Medical Sciences Campus (Puerto Rico)
  2. Department of Chemistry, University of Puerto Rico, Rio Piedras Campus (Puerto Rico)
  3. Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia (United States)

The genetically encoded fluorescent calcium-indicator protein GCaMP2 was crystallized in the calcium-saturated form. X-ray diffraction data were collected to 2.0 Å resolution and the structure was solved by molecular replacement. 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 Å resolution. The crystals belong to space group C2, with unit-cell parameters a = 126.1, b = 47.1, c = 68.8 Å, β = 100.5° and one GCaMP2 molecule in the asymmetric unit. The structure was phased by molecular replacement and refinement is currently under way.

OSTI ID:
22360584
Journal Information:
Acta Crystallographica. Section F, Vol. 64, Issue Pt 7; Other Information: PMCID: PMC2443961; PMID: 18607093; PUBLISHER-ID: bw5243; OAI: oai:pubmedcentral.nih.gov:2443961; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English