Unsharpened, unfiltered cryo-EM half-map.
Matching unsharpened, unfiltered cryo-EM half-map.
Configure inputs to begin
Set options on the left, then click “Submit job”.

Predict metal and water binding sites in protein structures using 3D convolutional neural networks (AllMetal3D + Water3D).

Validate protein structure quality with all-atom contact analysis, Ramachandran plots, rotamer assessment, and geometry checks.

Generate a downloadable PDBsum structural summary report archive for a single protein structure.

Calculate pairwise RMSD matrices for PDB structure ensembles with pyRMSD, including the condensed matrix and source statistics files.

Predict protein hydration sites from a structure using a diffusion model with ESM features and a confidence-filtering head.

Faithful static-mode Aggrescan3D tool for per-residue aggregation propensity analysis from a single protein structure.

Assess docking model quality by comparing predicted complexes against native references. DockQ v2.1.3 supports protein, nucleic-acid, and supported small-molecule interfaces with faithful native metrics.

Assign protein secondary structure using the DSSP algorithm. The gold standard for hydrogen bond-based structure assignment from coordinates.

Scoring function for interprotein interactions in AlphaFold2, AlphaFold3 and Boltz predictions. Calculates ipSAE, ipTM, pDockQ, pDockQ2, and LIS scores to assess protein-protein interface quality.

Analyze noncovalent interactions in protein-ligand complex structures with PLIP, including hydrogen bonds, hydrophobic contacts, pi interactions, salt bridges, water bridges, halogen bonds, and metal complexes.
LocScale performs local density scaling for cryo-EM maps. It sharpens map regions according to local signal and reference information rather than applying one global B-factor across the whole volume.
ProteinIQ runs LocScale on uploaded MRC/MAP files and returns the sharpened map plus the processing log and generated map files. The first release focuses on the standard LocScale command for local sharpening with half-map or full-map inputs. Feature-enhanced maps, coordinate-model refinement, hybrid model completion, MPI runs, and PDF reports are tracked for future support.
| Input | Description |
|---|---|
| Half Map 1 | First unsharpened, unfiltered half-map in MRC or MAP format. |
| Half Map 2 | Second matching unsharpened, unfiltered half-map. |
| Cryo-EM Map | Full unsharpened map for datasets without half-maps. |
| Mask | Optional MRC/MAP mask. LocScale estimates an FDR mask when this is omitted. |
| Reference Map | Optional MRC/MAP model map used directly as the LocScale reference. |
Half-map input is recommended when available because LocScale can use the pair for FSC-based resolution estimation.
The default settings match LocScale defaults for local sharpening: one CPU process, FDR threshold 0.01, averaging filter size 3, EMmerNet batch size 8, cube size 32, stride 16, and no input filtering. Optional resolution, window-size, FDR-window, FDR pre-filter, mask-threshold, and reference-map-resolution fields are passed to the corresponding LocScale command-line options only when set.
LocScale returns a primary sharpened MRC map. ProteinIQ also returns the LocScale log and generated processing files such as FDR masks or local-scaling diagnostic maps when LocScale writes them.
Open the returned MRC files in ChimeraX, Coot, or another cryo-EM map viewer for inspection.
C1 until symmetry-specific runtime checks are added.