130+ peer-reviewed publications, including 30 in Cell, Science & Nature
GPCR · Virus · Gene Editing · Antibody · Photosynthesis · Cilia/Flagella
Shanghai Institute of Materia Medica, CAS · Xu H et al.
ANTcryo™ and UltrAuFoil grids were used to reveal the Omicron mutant strain spike protein structure binding to the therapeutic antibody JMB2002 and receptor ACE2. The final resolutions achieved were 2.69 Å (using ANTcryo™) and 2.77 Å (using UltrAuFoil), demonstrating superior resolution performance.
Stanford University · Xu J, Chen G et al.
The Kobilka lab solved β2-adrenergic receptor structures with a calcineurin-fusion strategy. Antagonist- and agonist-bound samples were prepared on amorphous nickel-titanium alloy film (CryoMatrix, the predecessor of ANTcryo™) and reached 3.49 Å and 3.6 Å; the apo-state sample, prepared on a Quantifoil grid (R1.2/1.3, Au), reached 3.95 Å. The authors attribute the lower apo-state resolution to the intrinsic flexibility of the apo receptor, not to the support film.
ShanghaiTech University · Liu ZJ et al.
Three-dimensional cryo-EM structures of CB1 and CB2 cannabinoid receptors bound to G protein complexes. Sample preparation used ANTcryo™ grids (formerly CryoMatrix). Final resolutions: CB1 at 3.0 Å, CB2 at 2.9 Å.
Wang T, Liu ZJ et al. · ShanghaiTech University, iHuman Institute
The human olfactory receptor OR6A2 was successfully engineered into a functional protein for the first time, revealing its reversible covalent bond recognition mechanism for aldehyde odorants. A broadly conserved activation switch was discovered across Class II olfactory receptors.
S0092-8674(25)01430-8Xing L, Lu L et al. · Fudan University
First high-resolution structure of the early fusion intermediate of coronavirus S protein, revealing the precise conformation of the fusion peptide inserted into the host membrane after S2′ cleavage. Identifies this intermediate as an optimal antiviral target window.
DOI: 10.1016/j.cell.2025.01.012Xu P, Zhang F et al. · Broad Institute / MIT
Structures of 13 Fanzor proteins from 3 different organisms reveal the molecular diversity of eukaryotic gene-editing systems. The ωRNA binding interface is highly conserved, while TAM recognition and catalytic sites vary. The RuvC domain "Lid" loop undergoes conformational change upon guide-DNA pairing to regulate activation.
DOI: 10.1016/j.cell.2024.07.050Rosen LE, Starr TN et al. (53 authors) · University of Utah / Vir Biotechnology
Discovery of human monoclonal antibody VIR-7229 with unprecedented cross-reactivity against all sarbecovirus clades, including non-ACE2 bat sarbecoviruses, while potently neutralizing all SARS-CoV-2 variants since 2019. VIR-7229 tolerates extreme epitope diversification via high-affinity binding, receptor molecular mimicry, and backbone interactions.
DOI: 10.1016/j.cell.2024.09.026Dai J, Zhang R et al. · Washington University in St. Louis / Harvard Medical School
Cryo-EM structure of the hydroxyproline-rich mastigoneme, an extracellular filament isolated from Chlamydomonas cilia, at 3.1 Å. Two HRGPs form the filament — an MST1 polymer wrapped around a single MST3 — with hyperglycosylated poly(hydroxyproline) helices encased in carbohydrates. MST3 contains a PKD2-like transmembrane domain that forms a polycystin-like cation channel, explaining how mastigonemes are tethered to ciliary membranes.
DOI: 10.1016/j.cell.2024.03.005Hua T, Liu ZJ et al. · ShanghaiTech University, iHuman Institute
Three-dimensional cryo-EM structures of CB1 and CB2 bound to G protein molecules. Cryo-EM sample preparation used the ANTcryo™ grid. Final resolutions: 3.0 Å and 2.9 Å.
DOI: 10.1016/j.cell.2020.01.008Jin W, Xu RM et al. · Institute of Biophysics, CAS
Reveals the DNA targeting mechanism of human LINE-1, the only autonomously active retrotransposon. ORF2p functions as a structure-dependent endonuclease, binding upstream dsDNA and recognizing downstream fork/flap structures, suggesting L1 transposition "piggybacks" on chromosomal processes with non-canonical DNA structures.
DOI: 10.1126/science.adu3433Shen L, Wang W et al. · Institute of Botany, CAS
Coccolithophore PSI-fucoxanthin supercomplex at 2.79 Å resolution — 38 peripheral FCPI antennas, 819 pigment molecules, 95% quantum efficiency. Demonstrates ANTcryo™ capability for resolving ultra-large membrane protein complexes.
DOI: 10.1126/science.adv2132Peng R, Chang YW et al. · University of Pennsylvania
First revelation of influenza virus RNP as a right-handed antiparallel double helix with viral RNA wrapped in the minor groove. Visualized conformational changes of viral polymerase across functional states; nucleoprotein tail loop identified as a key drug target with candidate lead compounds.
DOI: 10.1126/science.adq7597Yin W, Xu H et al. · Shanghai Institute of Materia Medica, CAS
ANTcryo™ and UltrAuFoil grids were used to reveal the Omicron mutant strain spike protein structure binding to therapeutic antibody JMB2002 and receptor ACE2. Resolutions: 2.69 Å (ANTcryo™) vs 2.77 Å (UltrAuFoil).
Qiao A, Wu B et al. · Shanghai Institute of Materia Medica, CAS
Cryo-EM structures of the human glucagon receptor bound to both Gs and Gi heterotrimeric G proteins at 3.7 Å and 3.9 Å, revealing how a single class B GPCR engages two distinct G-protein subtypes — a structural framework for understanding glucagon signaling and rational drug design.
DOI: 10.1126/science.aaz5346Saito M, Zhang F et al. · Broad Institute of MIT and Harvard
First biochemical and structural characterization of Fanzor (Fz) proteins as eukaryotic RNA-guided DNA endonucleases — the evolutionary link between prokaryotic TnpB/Cas12 and eukaryotic gene regulation. The 2.7 Å cryo-EM structure reveals a conserved catalytic core despite diverse guide RNAs. Fanzor can be reprogrammed for human genome engineering, demonstrating that RNA-guided endonucleases exist across all three domains of life.
DOI: 10.1038/s41586-023-06356-2Duan J, Xu HE et al. · Shanghai Institute of Materia Medica, CAS
First complex structure of neurotensin receptor 1 (NTSR1) bound to GRK2, Gαq, and the arrestin-biased ligand SBI-553. GRK2 N-terminal helix docks into the open receptor cytoplasmic pocket formed by TM6 outward movement, analogous to G-protein binding. SBI-553 binds at the GRK2–NTSR1 interface, compatible with arrestin but clashing with Gαq — providing the structural basis for GRK2-mediated biased signaling.
DOI: 10.1038/s41586-023-06395-9Qu X, Wu B et al. · Shanghai Institute of Materia Medica, CAS
G protein-bound structures of the adhesion GPCRs ADGRD1 and ADGRF1 reveal how the stalk region preceding the first transmembrane helix acts as a tethered agonist, forming conserved interactions with the transmembrane domain shared across the aGPCR family. ADGRF1 also contains a specific lipid-binding site that may recognize the endogenous ligand synaptamide — highlighting the diverse signal transduction mechanisms of aGPCRs.
DOI: 10.1038/s41586-022-04580-wLin S, Wu B et al. · Shanghai Institute of Materia Medica, CAS
Cryo-EM structures of human mGlu2 and mGlu4 bound to heterotrimeric Gi protein. The G-protein-binding site formed by three intracellular loops and helices III and IV is distinct from all other GPCR structures, and the asymmetric dimer interface of the transmembrane domain proves crucial for receptor activation — providing the molecular basis for asymmetric signal transduction of class C GPCRs.
DOI: 10.1038/s41586-021-03495-2Xu J, Kobilka BK et al. · Stanford University
A novel calcineurin-fusion strategy for GPCR structural biology, enabling high-resolution cryo-EM studies. Represents the first ANTcryo™ publication from a leading international structural biology lab.
DOI: 10.1073/pnas.2414544121Sun D, Xu HE et al. · University of Science and Technology of China
First high-resolution structure (2.65–2.88 Å) of a GPCR–β-arrestin1–biased allosteric modulator SBI-553 ternary complex. Discovered a novel "loop engagement" coupling mode — NTSR1 ICL3 binds the central crest cavity of β-arrestin1, representing a previously unobserved arrestin-selective GPCR conformation.
DOI: 10.1038/s41422-025-01095-7Huang X, Sun F et al. · Institute of Biophysics, CAS
The foundational paper introducing the amorphous nickel-titanium alloy (ANTA) film as a revolutionary non-carbon support for cryo-EM. Demonstrated 18× lower protein adsorption, superior conductivity, and 2.36 Å resolution.
Data sourced from public ANTcryo™ user achievement records and verified against publisher databases. ANTcryo™ has supported dozens of high-impact publications — this list represents a curated selection.