@article {1580,
	title = {Crystallization and preliminary x-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2.},
	journal = {Acta Crystallographica. Section F, Structural Biology and Crystallization Communications},
	volume = {64},
	year = {2008},
	month = {2008 Jul 1},
	pages = {629-31},
	abstract = {<p>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.</p>
},
	keywords = {Amino Acid Sequence, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Crystallization, Green Fluorescent Proteins, Indicators and Reagents, Molecular Sequence Data, X-Ray Diffraction},
	issn = {1744-3091},
	doi = {10.1107/S1744309108016059},
	author = {Rodr{\'\i}guez Guilbe, Mar{\'\i}a M and Alfaro Malav{\'e}, Elisa C and Akerboom, Jasper and Marvin, Jonathan S and Looger, Loren L and Schreiter, Eric R}
}
