An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
In recent decades, significant progress has been made in construction and study of individual quantum systems consisting of the basic single matter and energy particles, i.e., atoms and photons, which show great potentials in quantum computation and communication. Here, we demonstrate that the quadruply-bonded Mo$_2$ unit of the complex can trap photons of visible light under ambient conditions, producing intense local electromagnetic (EM) field that features squeezed states, photon antibunching, and vacuum Rabi splitting. Our results show that both the electronic and vibrational states of the Mo$_2$ molecule are modified by coherent coupling with the scattered photons of the Mo$_2$ unit, as evidenced by the Rabi doublet4 and the Mollow triplet in the incoherent resonance fluorescence and the Raman spectra. The Mo$_2$ molecule, acting as an independent emitter-resonator integrated quantum system, allows optical experiments to be conducted in free space, enabling fundamental quantum phenomena to be observed through conventional spectroscopic instrumentation. This provides a new platform for study of field effects and quantum electrodynamics (QED) in the optical domain. The insights gained from this study advance our understanding in metal-metal bond chemistry, molecular physics and quantum optics, with applications in quantum information processing, optoelectronic devices and control of chemical reactivity.
The lateral stalk of ribosome is responsible for kingdom-specific binding of translation factors and activation of GTP hydrolysis that drives protein synthesis. In eukaryotes, the stalk is composed of acidic ribosomal proteins P0, P1 and P2 that constitute a pentameric P-complex in 1: 2: 2 ratio. We have determined the solution structure of the N-terminal dimerization domain of human P2 (NTD-P2), which provides insights into the structural organization of the eukaryotic stalk. Our structure revealed that eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. The two subunits of NTD-P2 form extensive hydrophobic interactions in the dimeric interface that buries 2400 Å 2 of solvent accessible surface area. We have showed that P1 can dissociate P2 homodimer spontaneously to form a more stable P1/P2 1 : 1 heterodimer. By homology modelling, we identified three exposed polar residues on helix-3 of P2 are substituted by conserved hydrophobic residues in P1. Confirmed by mutagenesis, we showed that these residues on helix-3 of P1 are not involved in the dimerization of P1/P2, but instead play a vital role in anchoring P1/P2 heterodimer to P0. Based on our results, models of the eukaryotic stalk complex were proposed.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
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