Performance Evaluation of Triangulation Based Range Sensors

The performance of 2D digital imaging systems depends on several factors related with both optical and electronic processing. These concepts have originated standards, which have been conceived for photographic equipment and bi-dimensional scanning systems, and which have been aimed at estimating different parameters such as resolution, noise or dynamic range. Conversely, no standard test protocols currently exist for evaluating the corresponding performances of 3D imaging systems such as laser scanners or pattern projection range cameras. This paper is focused on investigating experimental processes for evaluating some critical parameters of 3D equipment, by extending the concepts defined by the ISO standards to the 3D domain. The experimental part of this work concerns the characterization of different range sensors through the extraction of their resolution, accuracy and uncertainty from sets of 3D data acquisitions of specifically designed test objects whose geometrical characteristics are known in advance. The major objective of this contribution is to suggest an easy characterization process for generating a reliable comparison between the performances of different range sensors and to check if a specific piece of equipment is compliant with the expected characteristics

Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox

Interfering with disulfide bond formation impedes protein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques, the relationships of altered thiol redox and ER stress have been difficult to assess. We report that fluorescent lifetime measurements circumvented the crippling dimness of an ER-tuned fluorescent redox-responsive probe (roGFPiE), faithfully tracking the activity of the major ER-localized protein disulfide isomerase, PDI. In vivo lifetime imaging by time-correlated single-photon counting (TCSPC) recorded subtle changes in ER redox poise induced by exposure of mammalian cells to a reducing environment but revealed an unanticipated stability of redox to fluctuations in unfolded protein load. By contrast, TCSPC of roGFPiE uncovered a hitherto unsuspected reductive shift in the mammalian ER upon loss of luminal calcium, whether induced by pharmacological inhibition of calcium reuptake into the ER or by physiological activation of release channels. These findings recommend fluorescent lifetime imaging as a sensitive method to track ER redox homeostasis in mammalian cells