.[1] Nitric acid (HNO 3 ) is the dominant end product of NO x (= NO + NO 2 ) oxidation in the troposphere, and its dry deposition is considered to be a major removal pathway for the atmospheric reactive nitrogen. Here we present both field and laboratory results to demonstrate that HNO 3 deposited on ground and vegetation surfaces may undergo effective photolysis to form HONO and NO x , 1 -2 orders of magnitude faster than in the gas phase and aqueous phase. With this enhanced rate, HNO 3 photolysis on surfaces may significantly impact the chemistry of the overlying atmospheric boundary layer in remote low-NO x regions via the emission of HONO as a radical precursor and the recycling of HNO 3 deposited on ground surfaces back to NO x .

This protocol describes the reconstruction of biological molecules from the electron micrographs of single particles. Computation here is performed using the image-processing software SPIDER and can be managed using a graphical user interface, termed the SPIDER Reconstruction Engine. Two approaches are described to obtain an initial reconstruction: random-conical tilt and common lines. Once an existing model is available, reference-based alignment can be used, a procedure that can be iterated. Also described is supervised classification, a method to look for homogeneous subsets when multiple known conformations of the molecule may coexist.

As a ring-shaped adenosine triphosphatase (ATPase) machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo–electron microscopy (cryo-EM), we determined the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72–base pair DNA. NIPBL and DNA promote the engagement of cohesin’s ATPase head domains and ATP binding. The hinge domains of cohesin adopt an “open washer” conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA and provides insight into DNA entrapment by cohesin.