Data Logic Structure and Key Technologies on Intelligent High-precision Map

Taking autonomous driving and driverless as the research object,we discuss and define intelligent high-precision map.Intelligent high-precision map is considered as a key link of future travel,a carrier of real-time perception of traffic resources in the entire space-time range,and the criterion for the operation and control of the whole process of the vehicle.As a new form of map,it has distinctive features in terms of cartography theory and application requirements compared with traditional navigation electronic maps.Thus,it is necessary to analyze and discuss its key features and problems to promote the development of research and application of intelligent high-precision map.Accordingly,we propose an information transmission model based on the cartography theory and combine the wheeled robot’s control flow in practical application.Next,we put forward the data logic structure of intelligent high-precision map,and analyze its application in autonomous driving.Then,we summarize the computing mode of“Crowdsourcing+Edge-Cloud Collaborative Computing”,and carry out key technical analysis on how to improve the quality of crowdsourced data.We also analyze the effective application scenarios of intelligent high-precision map in the future.Finally,we present some thoughts and suggestions for the future development of this field.

A Novel Approach for Identifying the Heme-Binding Proteins from Mouse Tissues

Heme is a key cofactor in aerobic life, both in eukaryotes and prokaryotes. Because of the high reactivity of ferrous protoporphyrin IX, the reactions of heme in cells are often carried out through heme-protein complexes. Traditionally studies of heme-binding proteins have been approached on a case by case basis, thus there is a limited global view of the distribution of heme-binding proteins in different cells or tissues. The procedure described here is aimed at profiling heme-binding proteins in mouse tissues sequentially by 1) purification of heme-binding proteins by heme-agarose, an affinity chromatographic resin; 2) isolation of heme-binding proteins by SDS-PAGE or two-dimensional electrophoresis; 3) identification of heme-binding proteins by mass spectrometry. In five mouse tissues, over 600 protein spots were visualized on 2DE gel stained by Commassie blue and 154 proteins were identified by MALDI-TOF, in which most proteins belong to heme related. This methodology makes it possible to globally characterize the heme-binding proteins in a biological system.