# Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria

**Authors:** Nicole L. Inniss, George Minasov, Changsoo Chang, Kemin Tan, Youngchang Kim, Natalia Maltseva, Peter Stogios, Ekaterina Filippova, Karolina Michalska, Jerzy Osipiuk, Lukasz Jaroszewki, Adam Godzik, Alexei Savchenko, Andrzej Joachimiak, Wayne F. Anderson, Karla J. F. Satchell

PMC · DOI: 10.1128/mra.00200-25 · Microbiology Resource Announcements · 2025-05-20

## TL;DR

This paper describes solving 58 protein structures from bacteria to help develop better antibiotics.

## Contribution

The novel contribution is the high-throughput pipeline used to solve 58 new bacterial protein structures.

## Key findings

- 58 X-ray crystal structures of bacterial proteins were deposited.
- These structures are known antibiotic targets and reveal structural variation.
- The work supports future antibiotic discovery and modifications.

## Abstract

Antibiotic resistance remains a leading cause of severe infections worldwide. Small changes in protein sequence can impact antibiotic efficacy. Here, we report deposition of 58 X-ray crystal structures of bacterial proteins that are known targets for antibiotics, which expands knowledge of structural variation to support future antibiotic discovery or modifications.

## Full-text entities

- **Diseases:** infections (MESH:D007239)

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC12160482/full.md

## References

16 references — full list in the complete paper: https://tomesphere.com/paper/PMC12160482/full.md

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Source: https://tomesphere.com/paper/PMC12160482