In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion-coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA-CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with residues important for receptor interactions and sized to clamp one receptor dimer. CheW residues involved in kinase activation map to interfaces that orient the CheW clamps. CheA regulatory domains associate in crystals through conserved hydrophobic surfaces. Such CheA self-contacts align the CheW receptor clamps for binding receptor tips. Linking layers of ternary complexes with close-packed receptors generates a lattice with reasonable component ratios, cooperative interactions among receptors and accessible sites for modification enzymes.

Geometrical constraints to the electronic degrees of freedom within condensed-matter systems often give rise to topological quantum states of matter such as fractional quantum Hall states, topological insulators, and Weyl semimetals 1-3 . In magnetism, theoretical studies predict an entangled magnetic quantum state with topological ordering and fractionalized spin excitations, the quantum spin liquid 4 . In particular, the so-called Kitaev spin model 5 , consisting of a network of spins on a honeycomb lattice, is predicted to host Majorana fermions as its excitations. By means of a combination of specific heat measurements and inelastic neutron scattering experiments, we demonstrate the emergence of Majorana fermions in single crystals of α-RuCl 3 , an experimental realization of the Kitaev spin lattice. The specific heat data unveils a two-stage release of magnetic entropy that is characteristic of localized and itinerant Majorana fermions. The neutron scattering results corroborate this picture by revealing quasielastic excitations at low energies around the Brillouin zone centre and an hour-glass-like magnetic continuum at high energies. Our results confirm the presence of Majorana fermions in the Kitaev quantum spin liquid and provide an opportunity to build a unified conceptual framework for investigating fractionalized excitations in condensed matter 1,6-8 .Quantum spin liquids (QSLs) are an unconventional electronic phase of matter characterized by an absence of magnetic longrange order down to zero temperature. They are typically predicted to occur in geometrically frustrated magnets such as triangular, kagome, and pyrochlore lattices 4 , and typically display a macroscopic degeneracy that stabilizes a topologically ordered ground state. The Kitaev QSL state arises as an exact solution of the ideal two-dimensional (2D) honeycomb lattice with bond-directional Ising-type interactions (H = J γ K S γ i S γ j ; γ = x, y, z) on the three dis-

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Soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme that catalyzes the conversion of methane to methanol at ambient temperature using a nonheme, oxygen-bridged dinuclear iron cluster in the active site. Structural changes in the hydroxylase component (sMMOH) containing the diiron cluster caused by complex formation with a regulatory component (MMOB) and by iron reduction are important for the regulation of O2 activation and substrate hydroxylation. Structural studies of metalloenzymes using traditional synchrotron-based X-ray crystallography are often complicated by partial X-ray-induced photoreduction of the metal center, thereby obviating determination of the structure of the enzyme in pure oxidation states. Here, microcrystals of the sMMOH:MMOB complex from Methylosinus trichosporium OB3b were serially exposed to X-ray free electron laser (XFEL) pulses, where the ≤35 fs duration of exposure of an individual crystal yields diffraction data before photoreduction-induced structural changes can manifest. Merging diffraction patterns obtained from thousands of crystals generates radiation damage-free, 1.95 Å resolution crystal structures for the fully oxidized and fully reduced states of the sMMOH:MMOB complex for the first time. The results provide new insight into the manner by which the diiron cluster and the active site environment are reorganized by the regulatory protein component in order to enhance the steps of oxygen activation and methane oxidation. This study also emphasizes the value of XFEL and serial femtosecond crystallography (SFX) methods for investigating the structures of metalloenzymes with radiation sensitive metal active sites.

Although interfaces mediating protein-protein interactions are thought to be under strong evolutionary constraints, binding of the chemotaxis histidine kinase CheA to its phosphorylation target CheY suggests otherwise. The structure of Thermotoga maritima CheA domain P2 in complex with CheY reveals a different association than that observed for the same Escherichia coli proteins. Similar regions of CheY bind CheA P2 in the two systems, but the CheA P2 domains differ by an Ϸ90°rotation. CheA binds CheY with identical affinity in T. maritima and E. coli at the vastly different temperatures where the respective organisms live. Distinct sets of P2 residues mediate CheY binding in the two complexes; conservation patterns of these residues in CheA and compensations in CheY delineate two families of prokaryotic chemotaxis systems. A protein complex that has the same components and general function in different organisms, but an altered structure, indicates unanticipated complexity in the evolution of protein-protein interactions and cautions against extrapolating structural data from homologs.