• Journal of the Korea Institute of Information and Communication Engineering
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• v.23 no.9
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• pp.1060-1069
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• 2019

Pedestrian-based camera self-calibration methods are suitable for video surveillance systems since they do not require complex calibration devices or procedures. However, using arbitrary pedestrians as calibration targets may result in poor calibration accuracy due to the unknown height of each pedestrian. To solve this problem in the real surveillance environments, this paper proposes a novel Bayesian approach. By assuming known statistics on the height of pedestrians, we construct a probabilistic model that takes into account uncertainties in both the foot/head locations and the pedestrian heights, using foot-head homology. Since solving the model directly is infeasible, we use variational Bayesian inference, an approximate inference algorithm. Accordingly, this makes it possible to estimate the height of pedestrians and to obtain accurate camera parameters simultaneously. Experimental results show that the proposed algorithm is robust to noise and provides accurate confidence in the calibration.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.695-703
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• 1999

We have studied the stereospecificities of various pyridoxal 5'-phosphate (PLP) dependent enzymes for the hydrogen transfer between the C-4' of a bound coenzyme and the C-2 of a substrate in the transamination catalyzed by the enzymes. Stereospecificities reflect the structures of enzyme active-sites, in particular the geometrical relationship between the coenzyme-substrate Schiff base and the active site base participating in an $\alpha$-hydrogen abstraction. The PLP enzymes studied so far catalyze only a si-face specific (pro-S) hydrogen transfer. This stereochemical finding suggests that the PLP enzymes have the same topological active-site structures, and that the PLP enzymes have evolved divergently from a common ancestral protein. However, we found that o-amino acid aminotransferase, branched chain L-amino acid aminotransferase, and 4-amino-4-deoxychorismate lyase, which have significant sequence homology with one another, catalyze a re-face specific (pro-R) hydrogen transfer. We also showed that PLP-dependent amino acid racemases, which have no sequence homology with any aminotransferases, catalyze a non-stereospecific hydrogen transfer: the hydrogen transfer occurs on both faces of the planar intermediate. Crystallographical studies have shown that the catalytic base is situated on the re-face of the C-4' of the bound coenzyme in o-amino acid aminotransferase and branched chain L-amino acid aminotransferase, whereas the catalytic base is situated on the si-face in other aminotransferases (such as L-aspartate aminotransferase) catalyzing the si-face hydrogen transfer. Thus, we have clarified the stereospecificities of PLP enzymes in relation with the primary structures and three-dimensional structures of the enzymes. The characteristic stereospecificities of these enzymes for the hydrogen transfer suggest the convergent evolution of PLP enzymes.