Intrinsic Charge Dynamics in High-T_{c} AFeAs(O,F) Superconductors.

We report the first determination of the in-plane complex optical conductivity of 1111 high-T_{c} superconducting iron oxypnictide single crystals PrFeAs(O,F) and thin films SmFeAs(O,F) by means of conventional and microfocused infrared spectroscopy, ellipsometry, and time-domain THz transmission spectroscopy. A strong itinerant contribution is found to exhibit a dramatic difference in coherence between the crystal and the film. Using extensive temperature-dependent measurements of THz transmission, we identify a previously undetected 2.5-meV collective mode in the optical conductivity of SmFeAs(O,F), which is strongly suppressed at T_{c} and experiences an anomalous T-linear softening and narrowing below T^{*}≈110 K≫T_{c}. The suppression of the infrared absorption in the superconducting state reveals a large optical superconducting gap with a similar gap ratio 2Δ/k_{B}T_{c}≈7 in both materials, indicating strong pairing.

Field-Induced Magnonic Liquid in the 3D Spin-Dimerized Antiferromagnet Sr_{3}Cr_{2}O_{8}.

We report on ultrasound and magnetization studies in three-dimensional, spin-dimerized Sr_{3}Cr_{2}O_{8} as a function of temperature and external magnetic field up to 61 T. It is well established [A. A. Aczel et al., Phys. Rev. Lett. 103, 207203 (2009)] that this system exhibits a magnonic-superfluid phase between 30 and 60 T and below 8 K. By mapping ultrasound and magnetization anomalies as a function of magnetic field and temperature we establish that this superfluid phase is embedded in a domelike phase regime of a high-temperature magnonic liquid extending up to 18 K. Compared to thermodynamic results, our study indicates that the magnonic liquid could be characterized by an Ising-like order but has lost the coherence of the transverse components.

Erratum: Field-Induced Magnonic Liquid in the 3D Spin-Dimerized Antiferromagnet Sr_{3}Cr_{2}O_{8} [Phys. Rev. Lett. 116, 147201 (2016)].

This corrects the article DOI: 10.1103/PhysRevLett.116.147201.

Singlet-Triplet Excitations and Long-Range Entanglement in the Spin-Orbital Liquid Candidate FeSc2S4.

Theoretical models of the spin-orbital liquid (SOL) FeSc2S4 have predicted it to be in close proximity to a quantum critical point separating a spin-orbital liquid phase from a long-range ordered magnetic phase. Here, we examine the magnetic excitations of FeSc2S4 through time-domain terahertz spectroscopy under an applied magnetic field. At low temperatures an excitation emerges that we attribute to a singlet-triplet excitation from the SOL ground state. A threefold splitting of this excitation is observed as a function of applied magnetic field. As singlet-triplet excitations are typically not allowed in pure spin systems, our results demonstrate the entangled spin and orbital character of singlet ground and triplet excited states. Using experimentally obtained parameters we compare to existing theoretical models to determine FeSc2S4's proximity to the quantum critical point. In the context of these models, we estimate the characteristic length of the singlet correlations to be ξ/(a/2)≈8.2 (where a/2 is the nearest neighbor lattice constant), which establishes FeSc2S4 as a SOL with long-range entanglement.

Raman-scattering detection of nearly degenerate s-wave and d-wave pairing channels in iron-based Ba0.6K0.4Fe2As2 and Rb0.8Fe1.6Se2 superconductors.

We show that electronic Raman scattering affords a window into the essential properties of the pairing potential V(k,k') of iron-based superconductors. In Ba0.6K0.4Fe2As2 we observe band dependent energy gaps along with excitonic Bardasis-Schrieffer modes characterizing, respectively, the dominant and subdominant pairing channel. The d(x(2)-y(2)) symmetry of all excitons allows us to identify the subdominant channel to originate from the interaction between the electron bands. Consequently, the dominant channel driving superconductivity results from the interaction between the electron and hole bands and has the full lattice symmetry. The results in Rb(0.8)Fe(1.6)Se(2) along with earlier ones in Ba(Fe(0.939)Co(0.061))(2)As(2) highlight the influence of the Fermi surface topology on the pairing interactions.

Unconventional magnetostructural transition in CoCr2O4 at high magnetic fields.

The magnetic-field and temperature dependencies of the ultrasound propagation and magnetization of single-crystalline CoCr(2)O(4) have been studied in static and pulsed magnetic fields up to 14 and 62 T, respectively. Distinct anomalies with significant changes in the sound velocity and attenuation are found in this spinel compound at the onset of long-range incommensurate-spiral-spin order at T(s)=27 K and at the transition from the incommensurate to the commensurate states at T(l)=14 K, evidencing strong spin-lattice coupling. While the magnetization evolves gradually with the field, steplike increments in the ultrasound clearly signal a transition into a new magnetostructural state between 6.2 and 16.5 K and at high magnetic fields. We argue that this is a high-symmetry phase with only the longitudinal component of the magnetization being ordered, while the transverse helical component remains disordered. This phase is metastable in an extended H-T phase space.

NMR study in the iron-selenide Rb0.74Fe1.6Se2: determination of the superconducting phase as iron vacancy-free Rb0.3Fe2Se2.

77Se and 87Rb nuclear magnetic resonance (NMR) experiments on Rb0.74Fe1.6Se2 reveal clearly distinct spectra originating from a majority antiferromagnetic (AF) and a minority metallic-superconducting (SC) phase. The very narrow NMR line of the SC phase evidences the absence of Fe vacancies and any trace of AF order. The Rb content of the SC phase is deduced from intensity measurements identifying Rb(0.3(1))Fe2Se2 as the actual composition of the SC fraction. The resulting estimate of 0.15 electrons/Fe brings this class of superconductors 245 family closer to the other Fe-based superconductor families.

Universal exchange-driven phonon splitting in antiferromagnets.

We report a linear dependence of the phonon splitting Δω on the nondominant exchange coupling constant J(nd) in the antiferromagnetic transition-metal monoxides MnO, FeO, CoO, NiO, and in the frustrated antiferromagnetic oxide spinels CdCr(2)O(4), MgCr(2)O(4), and ZnCr(2)O(4). It directly confirms the theoretical prediction of an exchange-induced splitting of the zone-center optical phonon for the monoxides and explains the magnitude and the change of sign of the phonon splitting on changing the sign of the nondominant exchange also in the frustrated oxide spinels. The experimentally found linear relation [symbol:see text}Δω=ßJ(nd)S(2) with slope ß=3.7 describes the splitting for both systems and agrees with the observations in the antiferromagnets KCoF(3) and KNiF(3) with perovskite structure and negligible next-nearest neighbor coupling. The common behavior found for very different classes of cubic antiferromagnets suggests a universal dependence of the exchange-induced phonon splitting at the antiferromagnetic transition on the nondominant exchange coupling.

Nanoscale layering of antiferromagnetic and superconducting phases in Rb(2)Fe(4)Se(5) single crystals.

We studied phase separation in the single-crystalline antiferromagnetic superconductor Rb(2)Fe(4)Se(5) (RFS) using a combination of scattering-type scanning near-field optical microscopy and low-energy muon spin rotation (LE-µSR). We demonstrate that the antiferromagnetic and superconducting phases segregate into nanometer-thick layers perpendicular to the iron-selenide planes, while the characteristic in-plane size of the metallic domains reaches 10 µm. By means of LE-µSR we further show that in a 40-nm thick surface layer the ordered antiferromagnetic moment is drastically reduced, while the volume fraction of the paramagnetic phase is significantly enhanced over its bulk value. Self-organization into a quasiregular heterostructure indicates an intimate connection between the modulated superconducting and antiferromagnetic phases.

Magnetostructural transitions in a frustrated magnet at high fields.

Ultrasound and magnetization studies of bond-frustrated ZnCr(2)S(4) spinel are performed in static magnetic fields up to 18 T and in pulsed fields up to 62 T. At temperatures below the antiferromagnetic transition at T(N1)≈14 K, the sound velocity as a function of the magnetic field reveals a sequence of steps followed by plateaus indicating a succession of crystallographic structures with constant stiffness. At the same time, the magnetization evolves continuously with a field up to full magnetic polarization without any plateaus in contrast to geometrically frustrated chromium oxide spinels. The observed high-field magnetostructural states are discussed within a H-T phase diagram taking into account the field and temperature evolution of three coexisting spin structures and subsequent lattice transformations induced by the magnetic field.

Magnetic resonant mode in the low-energy spin-excitation spectrum of superconducting Rb2Fe4Se5 single crystals.

We have studied the low-energy spin-excitation spectrum of the single-crystalline Rb(2)Fe(4)Se(5) superconductor (T(c)=32 K) by means of inelastic neutron scattering. In the superconducting state, we observe a magnetic resonant mode centered at an energy of ℏω(res)=14 meV and at the (0.5 0.25 0.5) wave vector (unfolded Fe-sublattice notation), which differs from the ones characterizing magnetic resonant modes in other iron-based superconductors. Our finding suggests that the 245-iron selenides are unconventional superconductors with a sign-changing order parameter, in which bulk superconductivity coexists with the √5×√5 magnetic superstructure. The estimated ratios of ℏω(res)/k(B)T(c)≈5.1±0.4 and ℏω(res)/2Δ≈0.7±0.1, where Δ is the superconducting gap, indicate moderate pairing strength in this compound, similar to that in optimally doped 1111 and 122 pnictides.

Structural mechanism for statin inhibition of HMG-CoA reductase.

HMG-CoA (3-hydroxy-3-methylglutaryl-coenzyme A) reductase (HMGR) catalyzes the committed step in cholesterol biosynthesis. Statins are HMGR inhibitors with inhibition constant values in the nanomolar range that effectively lower serum cholesterol levels and are widely prescribed in the treatment of hypercholesterolemia. We have determined structures of the catalytic portion of human HMGR complexed with six different statins. The statins occupy a portion of the binding site of HMG-CoA, thus blocking access of this substrate to the active site. Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.

The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis.

The history and methods of membrane protein crystallization are described. The solution of the structure of the photosynthetic reaction center from the bacterium Rhodopseudomonas viridis is described, and the structure of this membrane protein complex is correlated with its function as a light-driven electron pump across the photosynthetic membrane. Conclusions about the structure of the photosystem II reaction center from plants are drawn, and aspects of membrane protein structure are discussed.

Crystal structure of DNA photolyase from Escherichia coli.

Photolyase repairs ultraviolet (UV) damage to DNA by splitting the cyclobutane ring of the major UV photoproduct, the cis, syn-cyclobutane pyrimidine dimer (Pyr <> Pyr). The reaction is initiated by blue light and proceeds through long-range energy transfer, single electron transfer, and enzyme catalysis by a radical mechanism. The three-dimensional crystallographic structure of DNA photolyase from Escherichia coli is presented and the atomic model was refined to an R value of 0.172 at 2.3 A resolution. The polypeptide chain of 471 amino acids is folded into an amino-terminal alpha/beta domain resembling dinucleotide binding domains and a carboxyl-terminal helical domain; a loop of 72 residues connects the domains. The light-harvesting cofactor 5,10-methenyltetrahydrofolylpolyglutamate (MTHF) binds in a cleft between the two domains. Energy transfer from MTHF to the catalytic cofactor flavin adenine dinucleotide (FAD) occurs over a distance of 16.8 A. The FAD adopts a U-shaped conformation between two helix clusters in the center of the helical domain and is accessible through a hole in the surface of this domain. Dimensions and polarity of the hole match those of a Pyr <> Pyr dinucleotide, suggesting that the Pyr <> Pyr "flips out" of the helix to fit into this hole, and that electron transfer between the flavin and the Pyr <> Pyr occurs over van der Waals contact distance.

Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.

Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.

Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria.

On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc1 complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an amino-terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc1 complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc1 complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology.

The leucine-rich repeat: a versatile binding motif.

Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.

Proteins with leucine-rich repeats.

Leucine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to beta-alpha structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.

APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.

In mitosis, the anaphase-promoting complex (APC) regulates the onset of sister-chromatid separation and exit from mitosis by mediating the ubiquitination and degradation of the securin protein and mitotic cyclins. With the use of a baculoviral expression system, we have reconstituted the ubiquitin ligase activity of human APC. In combination with Ubc4 or UbcH10, a heterodimeric complex of APC2 and APC11 is sufficient to catalyze the ubiquitination of human securin and cyclin B1. However, the minimal APC2/11 ubiquitin ligase module does not possess substrate specificity, because it also ubiquitinates the destruction box deletion mutants of securin and cyclin B1. Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly. Zn(2+)-binding and mutagenesis experiments indicate that APC11 binds Zn(2+) at a 1:3 M ratio. Unlike the two Zn(2+) ions of the canonical RING-finger motif, the third Zn(2+) ion of APC11 is not essential for its ligase activity. Surprisingly, with Ubc4 as the E2 enzyme, Zn(2+) ions alone are sufficient to catalyze the ubiquitination of cyclin B1. Therefore, the Zn(2+) ions of the RING finger family of ubiquitin ligases may be directly involved in catalysis.

Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.

BACKGROUND: Rab geranylgeranyltransferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. Unlike protein farnesyltransferase (FT) and type I geranylgeranyltransferase, which both prenylate monomeric small G proteins or short peptides, RabGGT can prenylate Rab only when Rab is in a complex with Rab escort protein (REP). RESULTS: The crystal structure of rat RabGGT at 2.0 A resolution reveals an assembly of four distinct structural modules. The beta subunit forms an alpha-alpha barrel that contains most of the residues in the active site. The alpha subunit consists of a helical domain, an immunoglobulin (Ig)-like domain, and a leucine-rich repeat (LRR) domain. The N-terminal region of the alpha subunit binds to the active site in the beta subunit; residue His2alpha directly coordinates a zinc ion. The prenyl-binding pocket of RabGGT is deeper than that in FT. CONCLUSIONS: LRR and Ig domains are often involved in protein-protein interactions; in RabGGT they might participate in the recognition and binding of REP. The binding of the N-terminal peptide of the alpha subunit to the active site suggests an autoinhibition mechanism that might contribute to the inability of RabGGT to recognize short peptides or Rab alone as its substrate. Replacement of residues Trp102beta and Tyr154beta in FT by Ser48beta and Leu99beta, respectively, in RabGGT largely determine the different lipid-binding specificities of the two enzymes.