All‐solid‐state (ASS) lithium metal batteries (LMBs) are considered the most promising next‐generation batteries due to their superior safety and high projected energy density. To access the practically desired high energy density of ASS LMBs, an ultrathin solid‐state electrolyte (SSE) film with fast ion‐transport capability presents as an irreplaceable component to reduce the proportion of inactive materials in ASS batteries. In this contribution, an ultrathin (60 µm), flexible, and free‐standing argyrodite (Li6PS5Cl) SSE film is designed through a self‐limited strategy. A chemically compatible cellulose membrane is employed as the self‐limiting skeleton that not only defined the thinness of the sulfide SSE film but also strengthened its mechanical properties. The ionic conductivity of the SSE film reaches up to 6.3 × 10−3 S cm−1 at room temperature, enabling rapid lithium‐ion transportation. The self‐limited SSE thin films are evaluated in various ASS LMBs with different types of cathode (sulfur and lithium titanate) and anode materials (lithium and lithium‐indium alloy) at both mold‐cell and pouch‐cell levels, demonstrating a stable performance and high‐rate capability. This study provides a general strategy for the rational design of an SSE thin film towards high‐energy‐density ASS batteries.

Unlike bibenzyls derived from the vascular plants, lunularic acid (LA), a key precursor for macrocyclic bisbibenzyl synthesis in nonvascular liverworts, exhibits the absence of one hydroxy group within the A ring. It was hypothesized that both polyketide reductase (PKR) and stilbenecarboxylate synthase 1 (STCS1) were involved in the LA biosynthesis, but the underlined mechanisms have not been clarified.This study used bioinformatics analysis with molecular, biochemical and physiological approaches to characterize STCS1s and PKRs involved in the biosynthesis of LA.The results indicated that MpSTCS1s from Marchantia polymorpha catalyzed both C2?C7 aldol-type and C6?C1 Claisen-type cyclization using dihydro-p-coumaroyl-coenzyme A (CoA) and malonyl-CoA as substrates to yield a C6-C2-C6 skeleton of dihydro-resveratrol following decarboxylation and the C6-C3-C6 type of phloretin in vitro. The protein-protein interaction of PKRs with STCS1 (PPI-PS) was revealed and proved essential for LA accumulation when transiently co-expressed in Nicotiana benthamiana. Moreover, replacement of the active domain of STCS1 with an 18-amino-acid fragment from the chalcone synthase led to the PPI-PS greatly decreasing and diminishing the formation of LA. The replacement also increased the chalcone formation in STCS1s.Our results highlight a previously unrecognized PPI in planta that is indispensable for the formation of LA.