4OY4
calcium-free CaMPARI v0.2
Summary for 4OY4
| Entry DOI | 10.2210/pdb4oy4/pdb |
| Descriptor | Chimera protein of Calmodulin, GPF-like protein EosFP, and Myosin light chain kinase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | calcium, fluorescent protein, photoconversion, integrator, engineered protein, calcium binding, fluorescent, transferase |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 1 |
| Total formula weight | 47665.34 |
| Authors | Fosque, B.F.,Schreiter, E.R. (deposition date: 2014-02-10, release date: 2015-02-18, Last modification date: 2024-11-06) |
| Primary citation | Fosque, B.F.,Sun, Y.,Dana, H.,Yang, C.T.,Ohyama, T.,Tadross, M.R.,Patel, R.,Zlatic, M.,Kim, D.S.,Ahrens, M.B.,Jayaraman, V.,Looger, L.L.,Schreiter, E.R. Neural circuits. Labeling of active neural circuits in vivo with designed calcium integrators. Science, 347:755-760, 2015 Cited by PubMed Abstract: The identification of active neurons and circuits in vivo is a fundamental challenge in understanding the neural basis of behavior. Genetically encoded calcium (Ca(2+)) indicators (GECIs) enable quantitative monitoring of cellular-resolution activity during behavior. However, such indicators require online monitoring within a limited field of view. Alternatively, post hoc staining of immediate early genes (IEGs) indicates highly active cells within the entire brain, albeit with poor temporal resolution. We designed a fluorescent sensor, CaMPARI, that combines the genetic targetability and quantitative link to neural activity of GECIs with the permanent, large-scale labeling of IEGs, allowing a temporally precise "activity snapshot" of a large tissue volume. CaMPARI undergoes efficient and irreversible green-to-red conversion only when elevated intracellular Ca(2+) and experimenter-controlled illumination coincide. We demonstrate the utility of CaMPARI in freely moving larvae of zebrafish and flies, and in head-fixed mice and adult flies. PubMed: 25678659DOI: 10.1126/science.1260922 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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