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Physics News Update
Number 646, July 16, 2003 by Phillip F. Schewe, Ben Stein, and James Riordon

Photonic Crystal Shifts Energy

Photonic crystals are artificial structures, sometimes consisting of stacked rods, or arrays of holes bored into a solid, which permit light in some wavelength bands to pass through while rejecting light at other bands.

New work at Sandia National Lab indicates that a photonic crystal made from half-micron-diameter tungsten rods, excited by thermal heating, suppresses light at longer wavelengths and re-emits light at a shorter wavelength band, one that may be more useful for such technological applications as photovoltaic power generation, or building a better lightbulb.

Shawn Lin and his Sandia colleagues, in the course of their studies of photonic crystals, have seemed to challenge the venerable formulation, made by Max Planck a hundred years ago, of what kind of emission spectrum a body should have. The Sandia photonic crystal seems to emit between 4 and 10 times as much radiation in the near infrared than a body at that temperature (the sample had been heated to 1250 C) should be emitting. (Lin et al., Applied Physics Letters, 14 July 2003; Lin et al., Optics Letters, Sep.15, 2003.)

Picosecond X-ray Crystallography of a Protein

Picosecond x-ray crystallography of a protein has been demonstrated for the first time, by a multinational collaboration (Philip Anfinrud, NIH, PhilipA@intra.niddk.nih.gov), enabling atom-scale movies of an important biomolecule as it performs a speedy function. This accomplishment will be presented at the upcoming American Crystallographic Association meeting from July 26-31 in Cincinnati (see also Schotte et al., Science, 20 June 2003).

While crystallographers have previously obtained frozen snapshots of thousands of proteins, they have yet to capture the full range of motion in even a single protein. Previous x-ray movies of proteins have been on the nanosecond time scale, which is too slow for capturing the steps of many protein processes.

Recently, however, at the European Synchrotron and Radiation Facility (ESRF) in France, researchers made picosecond-scale movies of a mutant myoglobin molecule getting rid of a toxic carbon monoxide (CO) molecule. Myoglobin is the protein that stores oxygen in muscle tissue. The researchers chose to study a mutant version of the protein because the highly strained atomic structure in part of the protein causes it to get rid of a CO molecule much more quickly than does ordinary myoglobin.

To capture this process, they first sent a 1-ps pulse of laser light to the protein to eject the CO. Immediately afterward, they illuminated the protein with intense, 150-ps x-ray pulses from the ESRF synchrotron. Crucial to this process was the ability to isolate single x-ray pulses from the synchrotron. A CCD camera recorded the patterns from the successive x-ray pulses as they passed through the protein.

The resulting movie showed the CO migrating to various sites in the protein, with the myoglobin rearranging its shape to accommodate the expulsion of the CO. In addition to enabling researchers to study many important transitions in proteins, the picosecond time-scale of these movies is commensurate with the timescale of many molecular dynamics simulations, allowing for closer comparison between theory and experiment.


Tumor Fly-Through Movies

Researchers at Purdue University and the Imperial College of Science in London have created a real-time holographic system to acquire a fly-through movie of living tissue using infrared light and a special, semiconductor holographic film. The acquired images showed structure inside rat tumors that, with conventional techniques, would only be visible if the tumor was sectioned into thin slices or imaged with ionizing radiation.

The researchers created the fly-through movie using optical coherence imaging (OCI). OCI is related to the more widely known optical coherence tomography (OCT). However, OCT involves scanning a laser beam through a sample and gathering information point by point, which then must be assembled into a complete image. OCI, on the other hand, captures complete images of thin tissue sections that can be recorded directly with a video camera.

The key to the holographic OCI technique is a dynamic holographic film that filters out the scattered, incoherent background light but passes the coherent, full-frame images to a camera. Tissue readily reflects image-bearing infrared light, but it also strongly scatters the light, and without coherence filtering the scattered light would overwhelm the coherent pictures.

By adjusting the relative delay between the image beam and the reference beam in the OCI system's imaging interferometer, the researchers (Ping Yu, 765-494-3004, pingyu@physics.purdue.edu, David Nolte, 765-494-3013, nolte@physics.purdue.edu) could control the depth of the images and assemble a slice-by-slice tour through a tumor while leaving the tissue intact.

Application of the OCI technique to cultured rat tumors revealed structures that appeared to be necroses (regions of dead tissue) and calcifications much like those found in human cancers (see image).

Ultimately, the researchers explain, holographic OCI could offer a nondestructive alternative to x-rays and microsectioning methods for studying living tissue. (P. Yu et al., Applied Physics Letters, 21 July 2003.)