Compact Mach-Zehnder interferometer based on self-collimation of light in a silicon photonic crystal.

We demonstrate a compact silicon photonic crystal Mach-Zehnder interferometer operating in the self-collimation regime. By tailoring the photonic band structure such as to produce self-collimated beams, it is possible to design beam splitters and mirrors and combine these to a 20 x 20 microm(2) format. With transmission spectroscopy we find a pronounced unidirectional optical output, the output ratio being as high as 25 at the self-collimation wavelength. Furthermore, the self-collimated beams and the unidirectionality are clearly observed in real space using near-field and far-field optical microscopy. Interpretation of the optical data is strongly supported by different types of simulations.

Wavelength tuning of planar photonic crystals by local processing of individual holes.

Tuning of the resonant wavelength of a single hole defect cavity in planar photonic crystals was demonstrated using transmission spectroscopy. Local post-production processing of single holes in a planar photonic crystal is carried out after selectively opening a masking layer by focused ion beam milling. The resonance was blue-shifted by enlargement of selected holes using local wet chemical etching and red-shifted by infiltration with liquid crystals. This method can be applied to precisely control the resonant frequency, and can also be used for mode selective tuning.

Wavelength-sized, tunable nanocavity in deeply etched InP/InGaAsP/InP photonic crystals.

Wavelength-sized point defect cavities coupled to access waveguides are reported for deeply etched InP/InGaAsP/InP two-dimensional photonic crystals. The observed quality factor of 60 is comparable to those found for one-row defect Fabry-Perot cavities and for simple point defect cavities in membranes. The quality factor was changed by varying the number of rows of holes. Upon infiltration of the holes with liquid crystal, frequency tuning was demonstrated.

Blazed x-ray reflection gratings fabricated by electron beam lithography.

We show that blazed gratings with well-controlled extremely small vertical dimensions can be made in electronresist (PMMA) using electron beam lithography.

Comparison of the active sites of atropinesterase and some serine proteases by spin-labeling.

The side chain of the serine residue in the active center of atropinesterase (AtrE), alpha-chymotrypsin (Chymo), and subtilisin A (Sub) was labeled with two paramagnetic reporter groups of different size (label I or II, respectively) by sulfonylation with N-[3-(fluorosulfonyl)phenyl]-1-oxy-2,2,5,5-tetramethyl-pyrroline-3 -carboxamide or N-[6-(fluorosulfonyl)-2-naphthyl]-1-oxy-2,2,5,5-tetramethylpyrroline+ ++-3 -carboxamide. ESR spectra of labeled enzymes in 10 mM phosphate buffer, pH 7.4, were measured at temperatures between 133 and 298 K by using a home-built spectrometer operating in the absorption mode at 10-kHz field modulation. The spectra, in particular those at 276-298 K, were analyzed by computer simulation of the overall line shape according to the methods developed by Freed and co-workers, based on eigenfunction expansion. In the case of AtrE for both labels, the best agreement between experimental and simulated solution spectra was obtained with only one mobility component showing anisotropic, axially symmetric reorientation according to the Egelstaff jump-diffusion model. The axis of preferential reorientation was found to lie in the XZ plane at a polar angle of about 30 degrees with the X axis. The corresponding rotational correlation time (tau parallel) did not show appreciable viscosity/temperature (eta/T) dependence but had a constant value of 4.4 and 2.2 ns for labels I and II, respectively. The rotational correlation time associated with rotation around the axes perpendicular to that of preferential reorientation (tau perpendicular) showed the usual eta/T dependence and had a value of 22.0 ns at 276 K for both labels. The above results strongly suggest that in AtrE both nonpolar reporter groups reside in a pocket near the active serine. Contrary to the situation in AtrE, the overall mobility of the -N-O. fragments in Chymo and Sub was found to result from contributions of at least two distinct motional states, strongly and weakly immobilized. In going from label I to label II, the relative contribution of the latter state increases at the expense of that of the former. This is ascribed to an equilibrium between a relatively free state of the aromatic cores and a firmly bound position in the specificity pocket of these proteases. The apparently more rigid embedding of the spin-labels in the enzyme structure of AtrE suggests that the size of the nonpolar binding pocket in the active center region of this esterase allows a deeper penetration of the aromatic portions of the labels than is possible for the specificity pocket of Chymo or Sub.