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Chrimson photocurrent properties

Chrimson window and door photocurrent properties were studied in CHO cells by using a whole-cell patch clamp. Each opsin mutant was tested to determine the peak photocurrent and compare it with a panel of control opsins. The peak photocurrents were estimated using monoexponential fit analysis.

The S169A mutant had a reduced photocurrent density compared to WT Chrimson. It was similar to the CrChR2 stationary currents measured in HEK cells (15 + 7 pA/pF). The ChrimsonSA photocurrents were significantly smaller than those of WT Chrimson, but they were sufficiently large to induce action potentials in HEK cells in the presence of 635 nm light.

ChrimsonSA is a useful optogenetic tool for dual-color experiments. Its red-shifted absorption reflects the protonation of counterions. Its photocurrent properties are very similar to BR.

Chrimson emitting surface covered with conductive film

Chrimson is an excitable protein expressed in larval flies and in adult flies. It mediates a variety of sensory and behavioral processes that require red light. Moreover, it is found to be robustly expressed in larval flies. Experiments using a Chrimson expression cassette revealed that Chrimson can modulate the response to CO2 and light at different wavelengths. These findings suggest that Chrimson can also be used for the temporally precise stimulation of neurons.

Chrimson is expressed in the frontal motor cortex and in cortical neurons. A vertically structured flexible mLED emits 30 mW mm-2 of light. The high intensity of the light did not cause any tissue damage. In addition, the intensity of red light was high enough to stimulate living mouse whiskers. The wavelength used for this stimulation was 650 nm. The brain tissue of a mouse was also sliced and tissue analysis was performed. In this brain slice, chrimson (ChR2) was expressed in the frontal motor cortex.

In a previous study, researchers observed that Chrimson-expressing neurons started spiking in blue only when the blue light intensity exceeded 0.5 mW/mm 2. In addition, chromson-expressing neurons could be driven with high fidelity at a low Chimson spike probability. These results suggested that the blue spectrum may be a reliable signal source for neuroscientists.

Chrimson's low sequence similarity to ChRs has hampered molecular engineering

Chrimson is an essential protein in the nervous system, but its low sequence similarity to ChRs has limited its use for molecular engineering. Despite this, it displays excellent crystallographic properties and shows excellent stability in detergents. Its N-terminal domains, which are derived from CrChR1, mediate contacts between the layers in the lipidic cubic phase crystal, and are crucial for dimeric interactions. In addition, the N-terminal residues are involved in the formation of three disulfide bonds.

A recent mutation analysis of Chrimson revealed structural features that contributed to its red light sensitivity. These included the presence of a Schiff base and the distribution of polar residues in the binding pocket. These mechanistic insights were used to engineer a ChrimsonSA mutant with enhanced red light sensitivity and accelerated closing kinetics.

ChRs are light-activated ion channels that mediate cation permeation across cell membranes. Their ability to respond to red light makes them ideal for dual-color experiments. The crystal structure of Chrimson channelrhodopsin (C1C2), a red-light-activated channelrhodopsin from algae, reveals a dimeric structure with a putative ion permeation pathway for each protomer. With this information, researchers were able to molecularly interpret a large volume of data. They were also able to rationally design variants with blue-shifted absorption and charge-inverted anion selectivity.