Safety practices for the construction site during the COVID-19 pandemic Understandably, dependable contractors want to prove they can work safely and avert the spread of COVID-19 as they provide much-needed income and support the nation's critical infrastructure. After all, the construction industry employs close to 11.2 million people. And that’s in the United States alone. Massachusetts Institute of Technology researchers discovered that coronavirus-bearing droplets of various sizes could travel as far as 23 to 27 feet from their hosts after emission through a sneeze or cough. Evidence also suggests that the virus can stay active for many hours on surfaces like tools, counters, and doorknobs. Those factors highlight the critical importance of ensuring physical distancing among all workers and employees. In line with this, contractors and owners need to adopt and implement physical distancing protocols and post details of the said protocol on the site. COVID-19 safety practices need to be incorporated into task hazard assessments (THA) and job briefings. THAs should also determine if a single employee can carry out a task, and if not, what type of personal protective equipment (PPE) can help ensure everyone's safety. Work schedules can be modified by staggering shifts or alternate days of work. Implementing dedicated shifts can also dramatically reduce the number of employees on the site at any given time. Breaks should also be designed in a way that minimizes interactions. Nonessential personnel should be allowed to work from home whenever possible. Typical behaviors among workers should be modified to protect them. For instance, conventional contact greetings like fist bumps and handshakes have to be eliminated. Also, workers should be required to park at a safe distance from each other.


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The online meeting will feature more than 50 speakers, including invited and contributed talks, Protein Society awards, live poster presentations, thematic workshops on crucial topics such as diversity and inclusion, and networking opportunities. Proteins are the "work-horses" of all living cells, catalyzing all essential functions in a cell. The discovery of their structure, function and dynamics is essential to understand the molecular basis of life. While genetic information in the form of DNA has only 4 building blocks, proteins are much more complex as their "alphabet" consist of 20 letters in the form of 20 amino acids, strung together like necklace beads. Proteins can fold into an almost limitless variety of three-dimensional shapes and interact with each other to form large supercomplexes that act as molecular machines to carry out essential life functions. The function of proteins is therefore dependent on their amino acid composition, 3D conformation, interactions and the dynamics of the complexes. Proteins perform myriad roles in the body, catalyzing all vital metabolic reactions essential to life. Examples include energy generation by respiration and photosynthesis, cell-cell recognition, import and export of products into cells, cell-cell recognition, DNA synthesis and repair, nerve function, smelling, tasting, hearing, vision to name just a few. In addition to providing the structural framework all tissues, proteins maintain proper pH and fluid balance and play a central role in the body's immune system. When protein function goes awry, it can lead to a broad array of serious diseases. Researchers have worked to develop drugs that can act on proteins, binding with them and altering, enhancing or in some cases, deactivating their functions. To accomplish this, a detailed map of the protein's molecular organization is needed. One of the most powerful techniques for investigating protein structure is through X-ray crystallography. Here, a sample of interest is crystalized, then interrogated with a beam of incident X-rays. When these X-rays strike the sample, the light is diffracted by the crystalline arrangement of atoms in the sample, and the patterns of diffracted X-ray light are caught on a detector-screen. By interrogating the crystal in all possible orientations with the X-rays, a detailed, three-dimensional portrait of the protein's structure can be determined by X-ray crystallography. The technique has been an exceptional boon to science, helping researchers to explore the inner workings of biological molecules, including drugs, vitamins, proteins and nucleic acids such as DNA. X-ray crystallography remains an essential method for characterizing the atomic structure of new materials and their properties as well as assisting in the design and validation of new pharmaceutical drugs. One major drawback in the past was been the fact that X-rays damage molecules when they interact with them, destroying the molecule the molecule under examination. This X-ray damage can be slowed down by freezing the crystals and collecting data at very low temperatures, however only a static picture of the frozen protein can the thereby ne obtained. Fromme and her team of colleagues at ASU as well as their national and international collaborators have pioneered a radically new version of X-ray crystallography, one which extends to the extreme the method's capacity to peer deeply into matter at the atomic scale.