Insights into current bio-processes and future perspectives of carbon-neutral treatment of industrial organic wastewater: A critical review.

With the rise of the concept of carbon neutrality, the current wastewater treatment process of industrial organic wastewater is moving towards the goal of energy conservation and carbon emission reduction. The advantages of anaerobic digestion (AD) processes in industrial organic wastewater treatment for bio-energy recovery, which is in line with the concept of carbon neutrality. This study summarized the significance and advantages of the state-of-the-art AD processes were reviewed in detail. The application of expanded granular sludge bed (EGSB) reactors and anaerobic membrane bioreactor (AnMBR) were particularly introduced for the effective treatment of industrial organic wastewater treatment due to its remarkable prospect of engineering application for the high-strength wastewater. This study also looks forward to the optimization of the AD processes through the enhancement strategies of micro-aeration pretreatment, acidic-alkaline pretreatment, co-digestion, and biochar addition to improve the stability of the AD system and energy recovery from of industrial organic wastewater. The integration of anaerobic ammonia oxidation (Anammox) with the AD processes for the post-treatment of nitrogenous pollutants for the industrial organic wastewater is also introduced as a feasible carbon-neutral process. The combination of AnMBR and Anammox is highly recommended as a promising carbon-neutral process for the removal of both organic and inorganic pollutants from the industrial organic wastewater for future perspective. It is also suggested that the AD processes combined with biological hydrogen production, microalgae culture, bioelectrochemical technology and other bio-processes are suitable for the low-carbon treatment of industrial organic wastewater with the concept of carbon neutrality in future.

Electrically Tunable Two-Color Cholesteric Laser.

Two-color lasing emission from an asymmetric structure, consisting of two dye-doped cholesteric liquid crystal (DD-CLC) layers separated by a transparent interlayer, is demonstrated. The DD-CLC mixtures have different reflection bands with long-wavelength band edges located at the green and red wavelengths of the visible spectrum, respectively. For the laser action, the CLC hosts provide the feedback, and the fluorescent laser dyes represent the active medium. When the stacked structure is optically pumped above the threshold, two simultaneous laser lines separated by 123 nm are observed at the long-wavelength band edges of the DD-CLC mixtures. The influence of an electric field on lasing behavior is also analyzed and discussed in terms of the reflection spectrum and laser action. The results show a reversible tuning of the reflection band, accompanied by a modification of the lasing characteristics under the application of an external field. Above a specific threshold voltage, one of the emission lines is suppressed and the other is conserved. With a further increase in the voltage, both laser emissions are entirely inhibited. The investigated structure demonstrates a simple technique to obtain an electrically tunable multi-wavelength laser, which might pave the way for a new generation of organic laser sources.

Virus structures revealed by advanced cryoelectron microscopy methods.

Before the resolution revolution, cryoelectron microscopy (cryo-EM) single-particle analysis (SPA) already achieved resolutions beyond 4 Å for certain icosahedral viruses, enabling ab initio atomic model building of these viruses. As the only samples that achieved such high resolution at that time, cryo-EM method development was closely intertwined with the improvement of reconstructions of symmetrical viruses. Viral morphology exhibits significant diversity, ranging from small to large, uniform to non-uniform, and from containing single symmetry to multiple symmetries. Furthermore, viruses undergo conformational changes during their life cycle. Several methods, such as asymmetric reconstruction, Ewald sphere correction, cryoelectron tomography (cryo-ET), and sub-tomogram averaging (STA), have been developed and applied to determine virus structures in vivo and in vitro. This review outlines current advanced cryo-EM methods for high-resolution structure determination of viruses and summarizes accomplishments obtained with these approaches. Moreover, persisting challenges in comprehending virus structures are discussed and we propose potential solutions.

Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity.

Amyloid-like assembly is not only associated with pathological events, but also leads to the development of novel nanomaterials with unique properties. Herein, using Fmoc diphenylalanine peptide (Fmoc-F-F) as a minimalistic model, we found that histidine can modulate the assembly behavior of Fmoc-F-F and induce enzyme-like catalysis. Specifically, the presence of histidine rearranges the ß structure of Fmoc-F-F to assemble nanofilaments, resulting in the formation of active site to mimic peroxidase-like activity that catalyzes ROS generation. A similar catalytic property is also observed in Aß assembled filaments, which is correlated with the spatial proximity between intermolecular histidine and F-F. Notably, the assembled Aß filaments are able to induce cellular ROS elevation and damage neuron cells, providing an insight into the pathological relationship between Aß aggregation and Alzheimer's disease. These findings highlight the potential of histidine as a modulator in amyloid-like assembly of peptide nanomaterials exerting enzyme-like catalysis.

Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1.

Chromatin inheritance entails de novo nucleosome assembly after DNA replication by chromatin assembly factor-1 (CAF-1). Yet direct knowledge about CAF-1's histone binding mode and nucleosome assembly process is lacking. In this work, we report the crystal structure of human CAF-1 in the absence of histones and the cryo-electron microscopy structure of CAF-1 in complex with histones H3 and H4. One histone H3-H4 heterodimer is bound by one CAF-1 complex mainly through the p60 subunit and the acidic domain of the p150 subunit. We also observed a dimeric CAF-1-H3-H4 supercomplex in which two H3-H4 heterodimers are poised for tetramer assembly and discovered that CAF-1 facilitates right-handed DNA wrapping of H3-H4 tetramers. These findings signify the involvement of DNA in H3-H4 tetramer formation and suggest a right-handed nucleosome precursor in chromatin replication.

The reduction of FIB damage on cryo-lamella by lowering energy of ion beam revealed by a quantitative analysis.

Focused ion beam (FIB) is widely used for thinning frozen cells to produce lamellae for cryo-electron microscopy imaging and for protein structures study in vivo. However, FIB damages the lamellae and a quantitative experimental analysis of the damage is lacking. We used a 30-keV gallium FIB to prepare lamellae of a highly concentrated icosahedral virus sample. The viruses were grouped according to their distance from the surface of lamellae and reconstructed. Damage to the approximately 20-nm-thick outermost lamella surface was similar to that from exposure to 16 e-/Å2 in a 300-kV cryo-electron microscope at high-resolution range. The damage was negligible at a depth beyond 50 nm, which was reduced to 30 nm if 8-keV Ga+ was used during polishing. We designed extra steps in the reconstruction refinement to maximize undamaged signals and increase the resolution. The results demonstrated that low-energy beam polishing was essential for high-quality thinner lamellae.

Structure of Semliki Forest virus in complex with its receptor VLDLR.

Semliki Forest virus (SFV) is an alphavirus that uses the very-low-density lipoprotein receptor (VLDLR) as a receptor during infection of its vertebrate hosts and insect vectors. Herein, we used cryoelectron microscopy to study the structure of SFV in complex with VLDLR. We found that VLDLR binds multiple E1-DIII sites of SFV through its membrane-distal LDLR class A (LA) repeats. Among the LA repeats of the VLDLR, LA3 has the best binding affinity to SFV. The high-resolution structure shows that LA3 binds SFV E1-DIII through a small surface area of 378 Å2, with the main interactions at the interface involving salt bridges. Compared with the binding of single LA3s, consecutive LA repeats around LA3 promote synergistic binding to SFV, during which the LAs undergo a rotation, allowing simultaneous key interactions at multiple E1-DIII sites on the virion and enabling the binding of VLDLRs from divergent host species to SFV.

Near-atomic architecture of Singapore grouper iridovirus and implications for giant virus assembly.

Singapore grouper iridovirus (SGIV), one of the nucleocytoviricota viruses (NCVs), is a highly pathogenic iridovirid. SGIV infection results in massive economic losses to the aquaculture industry and significantly threatens global biodiversity. In recent years, high morbidity and mortality in aquatic animals have been caused by iridovirid infections worldwide. Effective control and prevention strategies are urgently needed. Here, we present a near-atomic architecture of the SGIV capsid and identify eight types of capsid proteins. The viral inner membrane-integrated anchor protein colocalizes with the endoplasmic reticulum (ER), supporting the hypothesis that the biogenesis of the inner membrane is associated with the ER. Additionally, immunofluorescence assays indicate minor capsid proteins (mCPs) could form various building blocks with major capsid proteins (MCPs) before the formation of a viral factory (VF). These results expand our understanding of the capsid assembly of NCVs and provide more targets for vaccine and drug design to fight iridovirid infections.

Dual-Wavelength Lasing with Orthogonal Circular Polarizations Generated in a Single Layer of a Polymer-Cholesteric Liquid Crystal Superstructure.

We investigate the laser emission from a polymer-cholesteric liquid crystal superstructure with coexisting opposite chiralities fabricated by refilling a right-handed polymeric scaffold with a left-handed cholesteric liquid crystalline material. The superstructure exhibits two photonic band gaps corresponding to the right- and left-circularly polarized light. By adding a suitable dye, dual-wavelength lasing with orthogonal circular polarizations is realized in this single-layer structure. The wavelength of the left-circularly polarized laser emission is thermally tunable, while the wavelength of the right-circularly polarized emission is relatively stable. Due to its relative simplicity and tunability characteristics, our design might have broad application prospects in various fields of photonics and display technology.

Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA.

Cryo-electron tomography is a major tool used to study the structure of protein complexes in situ. However, the throughput of tilt-series image data collection is still quite low. Here, we show that GisSPA, a GPU accelerated program, can translationally and rotationally localize the target protein complex in cellular lamellae, as prepared with a focused ion beam, using single cryo-electron microscopy images without tilt-series, and reconstruct the protein complex at near-atomic resolution. GisSPA allows high-throughput data collection without the acquisition of tilt-series images and reconstruction of the tomogram, which is essential for high-resolution reconstruction of asymmetric or low-symmetry protein complexes. We demonstrate the power of GisSPA with 3.4-Å and 3.9-Å resolutions of resolving phycobilisome and tetrameric photosystem II complex structures in cellular lamellae, respectively. In this work, we present GisSPA as a practical tool that facilitates high-resolution in situ protein structure determination.

In situ structure of the red algal phycobilisome-PSII-PSI-LHC megacomplex.

In oxygenic photosynthetic organisms, light energy is captured by antenna systems and transferred to photosystem II (PSII) and photosystem I (PSI) to drive photosynthesis1,2. The antenna systems of red algae consist of soluble phycobilisomes (PBSs) and transmembrane light-harvesting complexes (LHCs)3. Excitation energy transfer pathways from PBS to photosystems remain unclear owing to the lack of structural information. Here we present in situ structures of PBS-PSII-PSI-LHC megacomplexes from the red alga Porphyridium purpureum at near-atomic resolution using cryogenic electron tomography and in situ single-particle analysis4, providing interaction details between PBS, PSII and PSI. The structures reveal several unidentified and incomplete proteins and their roles in the assembly of the megacomplex, as well as a huge and sophisticated pigment network. This work provides a solid structural basis for unravelling the mechanisms of PBS-PSII-PSI-LHC megacomplex assembly, efficient energy transfer from PBS to the two photosystems, and regulation of energy distribution between PSII and PSI.

Basis of the H2AK119 specificity of the Polycomb repressive deubiquitinase.

Repression of gene expression by protein complexes of the Polycomb group is a fundamental mechanism that governs embryonic development and cell-type specification1-3. The Polycomb repressive deubiquitinase (PR-DUB) complex removes the ubiquitin moiety from monoubiquitinated histone H2A K119 (H2AK119ub1) on the nucleosome4, counteracting the ubiquitin E3 ligase activity of Polycomb repressive complex 1 (PRC1)5 to facilitate the correct silencing of genes by Polycomb proteins and safeguard active genes from inadvertent silencing by PRC1 (refs. 6-9). The intricate biological function of PR-DUB requires accurate targeting of H2AK119ub1, but PR-DUB can deubiquitinate monoubiquitinated free histones and peptide substrates indiscriminately; the basis for its exquisite nucleosome-dependent substrate specificity therefore remains unclear. Here we report the cryo-electron microscopy structure of human PR-DUB, composed of BAP1 and ASXL1, in complex with the chromatosome. We find that ASXL1 directs the binding of the positively charged C-terminal extension of BAP1 to nucleosomal DNA and histones H3-H4 near the dyad, an addition to its role in forming the ubiquitin-binding cleft. Furthermore, a conserved loop segment of the catalytic domain of BAP1 is situated near the H2A-H2B acidic patch. This distinct nucleosome-binding mode displaces the C-terminal tail of H2A from the nucleosome surface, and endows PR-DUB with the specificity for H2AK119ub1.

Addressing compressive deformation of proteins embedded in crystalline ice.

For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions.

The deterioration of starch physiochemical and minerals in high-quality indica rice under low-temperature stress during grain filling.

Low temperatures during the grain-filling phase have a detrimental effect on both the yield and quality of rice grains. However, the specific repercussions of low temperatures during this critical growth stage on grain quality and mineral nutrient composition in high-quality hybrid indica rice varieties have remained largely unexplored. The present study address this knowledge gap by subjecting eight high-quality indica rice varieties to two distinct temperature regimes: low temperature (19°C/15°C, day/night) and control temperature (28°C/22°C) during their grain-filling phase, and a comprehensive analysis of various quality traits, with a particular focus on mineral nutrients and their interrelationships were explored. Exposure of rice plants to low temperatures during early grain filling significantly impacts the physicochemical and nutritional properties. Specifically, low temperature increases the chalkiness rate and chalkiness degree, while decreases starch and amylopectin content, with varying effects on amylose, protein, and gelatinization temperature among rice varieties. Furthermore, crucial parameters like gelatinization enthalpy (ΔH), gelatinization temperature range (R), and peak height index (PHI) all significantly declined in response to low temperature. These detrimental effects extend to rice flour pasting properties, resulting in reduced breakdown, peak, trough, and final viscosities, along with increased setback. Notably, low temperature also had a significant impact on the mineral nutrient contents of brown rice, although the extent of this impact varied among different elements and rice varieties. A positive correlation is observed between brown rice mineral nutrient content and factors such as chalkiness, gelatinization temperature, peak viscosity, and breakdown, while a negative correlation is established with amylose content and setback. Moreover, positive correlations emerge among the mineral nutrient contents themselves, and these relationships are further accentuated in the context of low-temperature conditions. Therefore, enhancing mineral nutrient content and increasing rice plant resistance to chilling stress should be the focus of breeding efforts to improve rice quality.

Interface characteristics of graphene/ZnS hybrid-dimensional heterostructures.

Graphene/ZnS hybrid-dimensional heterostructure is an excellent combination to regulate and improve the conductivity and sensitivity of components, in which the interface effects have crucial impacts on the performance of devices. In this work, we investigate the interface characteristics of Graphene/ZnS 2D/3D heterostructures. X-ray photoelectron spectra show that the ZnS binding energy shifts to lower energy by 0.3 eV after forming heterojunction with graphene. The fluorescence and absorption spectra confirm the luminescence enhancement and blue-shift of the absorbance edge of ZnS caused by graphene. The composition of Graphene/ZnS heterostructure facilitates separation and transfer of spatial charges, resulting in rapid electron transport.

Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli.

Bacterial lipoproteins perform a diverse array of functions including bacterial envelope biogenesis and microbe-host interactions. Lipoproteins in gram-negative bacteria are sorted to the outer membrane (OM) via the localization of lipoproteins (Lol) export pathway. The ATP-binding cassette (ABC) transporter LolCDE initiates the Lol pathway by selectively extracting and transporting lipoproteins for trafficking. Here, we report cryo-EM structures of LolCDE in apo, lipoprotein-bound, and AMPPNP-bound states at a resolution of 3.5 to 4.2 Å. Structure-based disulfide crosslinking, photo-crosslinking, and functional complementation assay verify the apo-state structure and reveal the molecular details regarding substrate selectivity and substrate entry route. Our studies snapshot 3 functional states of LolCDE in a transport cycle, providing deep insights into the mechanisms that underlie LolCDE-mediated lipoprotein sorting in E. coli.