WebThe crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 Å resolution and refined to a crystallographic R factor of 24.2 percent. The complex is stabilized by an extensive network of hydrogen bonds between the protein and the sugar-phosphate backbone. WebApr 12, 2024 · When Sc content is increased beyond the eutectic point, grain size decreases more significantly. An addition of 0.7 wt.% Sc can refine the grain to 40 μm. Figure 3 b shows that the grain size is fine and uniform, and the reduction rate reaches 95.3%. This difference in refinement results from refinement mechanism.
"ricin" 3D Models to Print - yeggi
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The three-dimensional structure of ricin at 2.8 A - ResearchGate
WebApr 7, 2024 · This biomimetic microstructure with a specific crystallographic texture not only enhances tensile strength but also facilitates the oriented adhesion and migration of bone cells. In particular, the fiber texture exposes the low-indexed Ti(0002) crystalline plane to air, allowing the formation of hydrophilic TiO 2 film with crystallographic anatase. WebMar 2, 2024 · Ricin A has three main regions: domain I consist of β -sheets, while domain II is an α -helical structure. Domain III plays a major role in dimer formation by binding to chain B. The active site of ricin contains highly conserved residues (Tyr80, Tyr123, Glu177, Trp211, and Arg180 ( Eswar et al., 2006 ); see Figure 3I ). WebA representation of the ricin protein based on X-ray crystallographic data is presented in Figure 27.4. Figure 27.4. Representation of the ricin protein derived from X-ray crystallographic data. The A-chain and B-chain are blue and orange, respectively. Random coil regions are strings, β-sheets are flat ribbons, and α-helices are coiled ribbons. how to slope roof revit