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[Preprint]. 2026 Jul 3:2026.06.29.733683. [Version 1] doi: 10.64898/2026.06.29.733683

zsasa: a Zig-based engine for high-throughput solvent accessible surface area at proteome scale

Tsubasa Nagae, Kentaro Tomii
PMCID: PMC13345171  PMID: 42427565

Abstract

Solvent accessible surface area (SASA) is widely used to describe protein stability, ligand binding, mutation effects, and protein–protein interfaces. As structural biology workloads expand to predicted-structure col-lections, trajectories, and large assemblies, SASA tools must combine reproducible calculation with high throughput, low memory use, and workflow-friendly input handling.

We present zsasa, a Zig-based SASA engine with command-line and Python interfaces. zsasa implements the established Shrake–Rupley and Lee–Richards algorithms, provides exact f64/f32 modes and an optional bitmask approximation, and supports batch and trajectory workflows, compressed structure inputs, and configurable atom classification including Chemical Component Dictionary (CCD)-based radii for non-standard components.

In matched Shrake–Rupley validation on 4,370 Escherichia coli AlphaFold Database structures, exact double-precision zsasa reproduced FreeSASA total SASA values to near numerical identity. In 10-thread batch benchmarks on the E. coli and 23,586-structure human AlphaFold collections, zsasa achieved a 2.94-fold speedup over a FreeSASA batch wrapper in exact f64 mode. In bitmask mode, zsasa reached up to a 9.70-fold speedup, using roughly 12.5% to 25% of the comparator peak memory. Trajectory benchmarks exceeded 1,000 frames/s at tens of megabytes of peak memory, and a 4.5-million-atom PDB stress-test file completed in less than 5 s. These results support zsasa as a practical tool for reproducible, low-memory generation of surface-derived structural features at large scale. zsasa is available under the MIT License at https://github.com/N283T/zsasa .

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