An evaluation tool kit of air quality micro-sensing units.

Recent developments in sensory and communication technologies have made the development of portable air-quality (AQ) micro-sensing units (MSUs) feasible. These MSUs allow AQ measurements in many new applications, such as ambulatory exposure analyses and citizen science. Typically, the performance of these devices is assessed using the mean error or correlation coefficients with respect to a laboratory equipment. However, these criteria do not represent how such sensors perform outside of laboratory conditions in large-scale field applications, and do not cover all aspects of possible differences in performance between the sensor-based and standardized equipment, or changes in performance over time. This paper presents a comprehensive Sensor Evaluation Toolbox (SET) for evaluating AQ MSUs by a range of criteria, to better assess their performance in varied applications and environments. Within the SET are included four new schemes for evaluating sensors' capability to: locate pollution sources; represent the pollution level on a coarse scale; capture the high temporal variability of the observed pollutant and their reliability. Each of the evaluation criteria allows for assessing sensors' performance in a different way, together constituting a holistic evaluation of the suitability and usability of the sensors in a wide range of applications. Application of the SET on measurements acquired by 25 MSUs deployed in eight cities across Europe showed that the suggested schemes facilitates a comprehensive cross platform analysis that can be used to determine and compare the sensors' performance. The SET was implemented in R and the code is available on the first author's website.CITI-SENSE, initiated in October 2012, is a four year Collaborative Project partly funded by the EU FP7-ENV-2012 under grant agreement 308524

The first structure function study of GH151 alpha l fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity

Fucosylated compounds are abundantly present in nature and are associated with many biological processes, therefore carrying great potential for use in medicine and biotechnology. Efficient ways to modify fucosylated compounds are still being developed. Promising results are provided by glycosyl hydrolases with transglycosylating activities, such as amp; 945; l fucosidase isoenzyme 2 from Paenibacillus amp; 8201;thiaminolyticus family GH151 of Carbohydrate Active enZYmes . Currently, there is no 3D structure representing this glycoside hydrolase family and only a few members have been investigated. Here, we present the first structure function study of a GH151 member, providing the key insights into its specific oligomerization and active site properties. According to the crystal structure, small angle X ray scattering data and catalytic investigation, this enzyme functions as a tetramer of a new type and represents the second known case of active site complementation among all amp; 945; l fucosidases. Mutation of the active site complementing residue histidine 503 to alanine confirmed its influence on amp; 945; l fucosidase activity and, specifically, on substrate binding. Several unique features of GH151 family amp; 945; l fucosidases were revealed, including the oligomerization pattern, active site accessibility and complementation, and substrate selectivity. Some common properties of GH151 glycosyl hydrolases then would be the overall three domain structure and conservation of the central domain loop 2 function, including its complementation role and the formation of the carbohydrate binding platform in the active site vicinit