Risk communication: lessons from an ethnographic, pragmatic, and Canadian regulatory perspective

In a regulatory context, it is important to understand how effective risk communication fits into the overall risk assessment, management, and decision-making process. This includes recognizing the intersections between risk analysis and the 3Ps: policy, politics, and publics, and understanding the barriers to effective communication. Risk communication is especially challenging when it requires the audience to follow and act on authoritative information or advice. Risk communicators must factor attributes such as risk perception, tolerance, and behaviors, and tailor the delivery of messages to diverse audiences. This paper captures the discourse from an intradepartmental workshop on risk communication with participants from Health Canada and the Public Health Agency of Canada. The workshop provided an opportunity to discuss and share references to existing frameworks, pertinent documents, and examples of effective risk communication strategies based on the authors' ethnographic and pragmatic experiences. The workshop aimed to strengthen risk communication by better understanding the value in collaborating with interdisciplinary teams, applying a systems thinking lens, and finding opportunities to experiment and evaluate risk communication strategies for regulatory purposes

The Crystal Structure of a Cyanobacterial Water-Soluble Carotenoid Binding Protein

AbstractCarotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to light harvesting, they perform an essential role in protecting against light-induced damage by quenching singlet oxygen, superoxide anion radicals, or triplet-state chlorophyll. We have determined the crystal structure of a water-soluble orange carotenoid protein (OCP) isolated from the cyanobacterium Arthrospira maxima at a resolution of 2.1 Å. OCP forms a homodimer with one carotenoid molecule per monomer. The carotenoid binding site is lined by a striking number of methionine residues. The structure reveals several possible ways in which the protein environment influences the spectral properties of the pigment and provides insight into how the OCP carries out its putative functions in photoprotection