Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 64, Issue -, Pages 629-631Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108016059
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Funding
- NCRR NIH HHS [P20 RR016439, 1P20RR16439-01] Funding Source: Medline
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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 angstrom resolution. The crystals belong to space group C2, with unit- cell parameters a = 126.1, b = 47.1, c = 68.8 angstrom, beta = 100.5 degrees and one GCaMP2 molecule in the asymmetric unit. The structure was phased by molecular replacement and refinement is currently under way.
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