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From three dimensional whispering gallery cavities of GaAs photonic quantum ring fabricated in hyperboloid drum shape by chemically assisted ion beam etching with the central active region diameter of 0.9 μm, we have observed single mode lasing near 838 nm with a record low injection threshold of 300 nA (Jth=47.1 A/cm2) in continuous wave operation at room temperature. This indicates that the quantum ring lasing phenomena associated with the three dimensional whispering gallery modes continue to persist, even at the submicron range overcoming the conventional two dimensional whispering gallery mode limit. [ABSTRACT FROM AUTHOR]

MutL is required to assist the mismatch repair protein MutS during initiation of the methyl-directed mismatch repair (MMR) response in various organisms ranging from prokaryotes to eukaryotes. Despite this necessity, the inherent propensity of MutL to aggregate has led to significant difficulties in determining its biological relationship with other MMR-related proteins. Here, we perform analysis on the thermostable MutL protein found in Thermotoga maritima MSB8 (TmL). Size exclusion chromatographic analysis indicates the lack of aggregated forms with the exception of a dimeric TmL. Small-angle X-ray scattering (SAXS) analysis reveals that the solution structures of the full-length TmL and its corresponding complexes with nucleotides and ssDNA undergo conformational changes. The elucidated TmL SAXS model is superimposed to the crystal structure of the C-terminal domain of Escherichia coli MutL. In addition, the N-terminal SAXS model of TmL exists as monomeric form, indicating that TmL has a structurally flexible N-terminal domain. TmL SAXS analysis can suggest a considerable possibility on a new 3D view of the previously unresolved full-length MutL molecule. [ABSTRACT FROM PUBLISHER]