forthcoming articles

We determined crystal structures of TCR 4414 A bound to HLA-A2â"presented p53Y220D and of the corresponding unbound wild-type and mutant p53â"HLA-A2 ligands, revealing that the Y220D driver mutation reshapes the peptide and renders a normally cryptic self-epitope visible to T cells. These structures explain how TCR 4414 A achieves high specificity for mutant p53 by minimizing interactions with conserved peptide regions and instead focusing on the central Y220D mutation, providing a structural basis for mutation-specific TCR immunotherapy.

Ultra-high-resolution crystallography combined with in-crystallo Co K-edge XANES shows that cobalamin retains octahedral cobalt coordination in both oxidized and reduced states. These results rule out radiation-induced Coâ"CN cleavage as the cause of the missing axial ligand in intrinsic factorâ"bound cobalamin.

Conformational dynamics in the melibiose/Na⁺ cotransporter MelB significantly influence the binding of the primary sugar substrate but have minimal effect on the co-substrate Na⁺. Na⁺ acts as an allosteric activator, increasing sugar affinity by stabilizing the inner barrier and constraining conformational flexibility.

Here we describe the determination of the highest resolution structure in the PDB at 0.43 Å resolution. Electron density maps reveal extensive deformation electron density that is completely accounted for by performing transferable aspherical atom refinements using the DiSCaMB library in BUSTER.

Here we describe a new to prepare grids for cryoEM in the sub millisecond time-scale.

Flawed protein-ligand X-ray structures can misdirect drug discovery based on PDB-deposited models. This review uses publicly available PDB examples to highlight potential pitfalls—from absent ligands to incorrect chemistry—and presents a practical validation approach to improve model reliability.

We report a room-temperature serial synchrotron X-ray (SSX) crystallography structure analysis of the Nitratidesulfovibrio vulgaris formate dehydrogenase AB (NvFdhAB), an enzyme that reduces CO₂ to formate.

Replacement soaking, also known as cross-soaking, is a compelling method for solving complex structures in cases where traditional soaking and co-crystallization approaches fail. This method is demonstrated with human tankyrase 2, and new crystal structures of complexes with nanomolar inhibitors and an analogue of the substrate NAD⁺ are reported.

In biological systems, hydrogels often arise through liquid–liquid phase separation, where biomolecular condensates can age into gel-like states. SAXS is a key technique to probe the molecular organization of these samples. This study introduces an in-vacuum Gel-Cell for SAXS-based structural analysis of a biologically derived hydrogel formed by the thermosensory prion-like domain of EARLY FLOWERING 3 and presents a three-component model to interpret the obtained data.

The oligomerization of B. melitensis bacterioferritin (BmBfr) was studied using X-ray crystallography, size-exclusion chromatography and thermal shift analysis. These techniques allowed the characterization of both apo and holo BmBfr, highlighting the impact of heme and pH on the oligomerization mechanism.

We present a fully automated, unattended cryo-EM pipeline that serves as an on-the-fly diagnostic tool, enabling rapid data-quality assessment and informed decision-making to maximize data-collection efficiency.

A series of 36 structures of the Neurospora crassa LPMO NcAA9D were refined against X-ray crystal datasets collected with increasing dose from a single crystal to provide insights into dose-dependent structural changes at the active site of the enzyme. The findings underscore the importance of minimizing accumulated dose during cryo-X-ray crystallographic studies of lytic polysaccharide monooxygenases to prevent the misinterpretation of radiation damage-related electron-density features.

LowDoseWizard is a guided SerialEM workflow for rapid and standardized setup of low-dose cryo-TEM imaging conditions for single-particle analysis and cryo-electron tomography.

The open and closed lid conformational states of class C sortase, which catalyzes the polymerization of endocarditis and biofilm-associated pili in E. faecalis, were captured in a single crystal. Communication between the flexible lid and the dynamic active-site (β7–β8) loop, along with their synchronized motions, regulates access to the active site for primary- and secondary-substrate binding.