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The metal-metal-bonded molecule [Bu4N][(HL)2Fe6(dmf)2] (Fe6) was previously shown to possess a thermally isolated spin S = 19/2 ground state and found to exhibit slow magnetization relaxation below a blocking temperature of ∼5 K [J. Am. Chem. selleckchem Soc.2015, 137, 13949-13956]. Here, we present a comprehensive spectroscopic investigation of this unique single-molecule magnet (SMM), combining ultrawideband field-swept high-field electron paramagnetic resonance (EPR) with frequency-domain Fourier-transform terahertz EPR to accurately quantify the spin Hamiltonian parameters of Fe6. Of particular importance is the near absence of a 4th-order axial zero-field splitting term, which is known to arise because of quantum mechanical mixing of spin states on account of the relatively weak spin-spin (superexchange) interactions in traditional polynuclear SMMs such as the celebrated Mn12-acetate. The combined high-resolution measurements on both powder samples and an oriented single crystal provide a quantitative measure of the isolated nature of the spin ground state in the Fe6 molecule, as well as additional microscopic insights into factors that govern the quantum tunneling of its magnetization. This work suggests strategies for improving the performance of polynuclear SMMs featuring direct metal-metal bonds and strong ferromagnetic spin-spin (exchange) interactions.The outbreak of COVID-19 caused a worldwide public health crisis. Large-scale population screening is an effective means to control the spread of COVID-19. Reverse transcription-polymerase chain reaction (RT-qPCR) and serology assays are the most available techniques for SARS-CoV-2 detection; however, they suffer from either less sensitivity and accuracy or low instrument accessibility for screening. To balance the sensitivity, specificity, and test availability, here, we developed enhanced colorimetry, which is termed as a magnetic pull-down-assisted colorimetric method based on the CRISPR/Cas12a system (M-CDC), for SARS-CoV-2 detection. By this method, SARS-CoV-2 RNA from synthetic sequences and cultured viruses can be detected by the naked eye based on gold nanoparticle (AuNP) probes, with a detection limit of 50 RNA copies per reaction. With CRISPR/Cas12a-assisted detection, SARS-CoV-2 can be specifically distinguished from other closely related viruses. M-CDC was further used to analyze 41 clinical samples, whose performance was 95.12%, consistent with that of an approved Clinical RT-qPCR Diagnosis kit. The developed M-CDC method is not dependent on sophisticated instruments, which makes it potentially valuable to be applied for SARS-CoV-2 screening under poor conditions.Protein molecules bring a rich functionality to the field of designed nanoscale architectures. High-symmetry protein cages are rapidly finding diverse applications in biomedicine, nanotechnology, and imaging, but methods for their reliable and predictable construction remain challenging. In this study we introduce an approach for designing protein assemblies that combines ideas and favorable elements adapted from recent work. Cubically symmetric cages can be created by combining two simpler symmetries, following recently established principles. Here, two different oligomeric protein components are brought together in a geometrically specific arrangement by their separate genetic fusion to individual components of a heterodimeric coiled-coil polypeptide motif of known structure. Fusions between components are made by continuous α-helices to limit flexibility. After a computational design, we tested 10 different protein cage constructions experimentally, two of which formed larger assemblies. One produced the intended octahedral cage, ∼26 nm in diameter, while the other appeared to produce the intended tetrahedral cage as a minor component, crystallizing instead in an alternate form representing a collapsed structure of lower stoichiometry and symmetry. Geometric distinctions between the two characterized designs help explain the different degrees of success, leading to clearer principles and improved prospects for the routine creation of nanoscale protein architectures using diverse methods.(1 - x)PbVO3-xBiCoO3 solid solutions with 0 ≤ x ≤ 1 were prepared at a high pressure of 5-6 GPa and a high temperature of 1223-1473 K. They adopt a polar tetragonal P 4mm structure for the 0 ≤ x ≤ 0.3 and 0.75 ≤ x ≤ 1 ranges with giant tetragonal distortions and a cubic Pm3̅m structure for the 0.4 ≤ x ≤ 0.7 range. High-temperature structural studies with synchrotron X-ray powder diffraction showed that polarization, calculated by the point-charge model, and the tetragonal distortion remained nearly constant in the x = 0.8 sample from 295 K up to the decomposition temperature of about 700 K. Magnetic and differential scanning calorimetry measurements showed that the Néel temperature, TN, nearly linearly decreased from 470 K for x = 1 to 250 K for x = 0.75 (with TN = 395 K for x = 0.9 and TN = 295 K for x = 0.8). Long-range magnetic ordering also takes place at TN = 44 K for x = 0. All other samples with 0.1 ≤ x ≤ 0.7 demonstrated spin-glass-like magnetic properties and notably reduced Weiss temperatures. Effective magnetic moments estimated for the x = 0.6, 0.65, and 0.7 cubic samples gave evidence that cobalt is present in the +2 and +3 oxidation states, and Co3+ cations take the low-spin state.This article describes a theoretical and computational study of the dynamical assembly of a protein shell around a complex consisting of many cargo molecules and long, flexible scaffold molecules. Our study is motivated by bacterial microcompartments, which are proteinaceous organelles that assemble around a condensed droplet of enzymes and reactants. As in many examples of cytoplasmic liquid-liquid phase separation, condensation of the microcompartment interior cargo is driven by flexible scaffold proteins that have weak multivalent interactions with the cargo. Our results predict that the shell size, amount of encapsulated cargo, and assembly pathways depend sensitively on properties of the scaffold, including its length and valency of scaffold-cargo interactions. Moreover, the ability of self-assembling protein shells to change their size to accommodate scaffold molecules of different lengths depends crucially on whether the spontaneous curvature radius of the protein shell is smaller or larger than a characteristic elastic length scale of the shell.
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