Monocular metasurface camera for passive single-shot 4D imaging.

It is a grand challenge for an imaging system to simultaneously obtain multi-dimensional light field information, such as depth and polarization, of a scene for the accurate perception of the physical world. However, such a task would conventionally require bulky optical components, time-domain multiplexing, and active laser illumination. Here, we experimentally demonstrate a compact monocular camera equipped with a single-layer metalens that can capture a 4D image, including 2D all-in-focus intensity, depth, and polarization of a target scene in a single shot under ambient illumination conditions. The metalens is optimized to have a conjugate pair of polarization-decoupled rotating single-helix point-spread functions that are strongly dependent on the depth of the target object. Combined with a straightforward, physically interpretable image retrieval algorithm, the camera can simultaneously perform high-accuracy depth sensing and high-fidelity polarization imaging over an extended depth of field for both static and dynamic scenes in both indoor and outdoor environments. Such a compact multi-dimensional imaging system could enable new applications in diverse areas ranging from machine vision to microscopy.

The structure of rice weevil pectin methylesterase.

Rice weevils (Sitophilus oryzae) use a pectin methylesterase (EC 3.1.1.11), along with other enzymes, to digest cell walls in cereal grains. The enzyme is a right-handed ß-helix protein, but is circularly permuted relative to plant and bacterial pectin methylesterases, as shown by the crystal structure determination reported here. This is the first structure of an animal pectin methylesterase. Diffraction data were collected to 1.8 Šresolution some time ago for this crystal form, but structure solution required the use of molecular-replacement techniques that have been developed and similar structures that have been deposited in the last 15 years. Comparison of the structure of the rice weevil pectin methylesterase with that from Dickeya dandantii (formerly Erwinia chrysanthemi) indicates that the reaction mechanisms are the same for the insect, plant and bacterial pectin methylesterases. The similarity of the structure of the rice weevil enzyme to the Escherichia coli lipoprotein YbhC suggests that the evolutionary origin of the rice weevil enzyme was a bacterial lipoprotein, the gene for which was transferred to a primitive ancestor of modern weevils and other Curculionidae. Structural comparison of the rice weevil pectin methylesterase with plant and bacterial enzymes demonstrates that the rice weevil protein is circularly permuted relative to the plant and bacterial molecules.