Molecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. Illumination at both wavelengths photobleaches red mEos3.2 molecules with a rate constant of k bl. The photoconversion of the on- to the off-state includes both internal and surface exposed protein structural changes, occurring in regions that lack crystal contacts in the orthorhombic crystal form. Illumination at 405 nm photoconverts mature mEos3.2 molecules from the green (G) state to the red (R) state with a photoconversion rate constant of k act. Furthermore, a comparison of droplet on demand, grease injection and Gas Dynamic Virtual Nozzle (GDVN) injection shows no significant differences in limiting resolution. We present a comparison of the data reduction and structure determination statistics for the two facilities which differ in flux, beam characteristics and detector technologies. proteins such as mEos3.2 (mEos2 is depicted here, PDB: 3S05) can be photoconverted from a green- emitting state to a red-emitting state by low levels of UV.
#Meos3.2 photoconvert serial#
We present X-ray crystal structures of the cis (on) state at 1.9 Angstrom resolution and the trans (off) state at a limiting resolution of 1.55 Angstrom from serial femtosecond crystallography experiments conducted at SPring-8 Angstrom Compact Free Electron Laser (SACLA) at 7.0 keV and 10.5 keV, and at Linac Coherent Light Source (LCLS) at 9.5 keV. Photo-conversion with illumination at 515 nm generates a meta-stable intermediate with neutral trans-chromophore structure that has a 4 h lifetime. The photochromic fluorescent protein Skylan-NS (Nonlinear Structured illumination variant mEos3.1H62L) is a reversibly photoswitchable fluorescent protein which has an unilluminated/ground state with an anionic and cis chromophore conformation and high fluorescence quantum yield.
Biologically Interesting Molecule Reference Dictionary (BIRD).
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