FLEXR-MSA: electron-density map comparisons of sequence-diverse structures.

ABSTRACT: Proteins with near-identical sequences often share similar static structures. Yet, comparing crystal structures is limited or even biased by what has been included or omitted in the deposited model. Information about unique dynamics is often hidden in electron-density maps. Currently, automatic map comparisons are limited to sequence-identical structures. To overcome this limitation, we developed FLEXR-MSA, which enables unbiased electron-density map comparisons of sequence-diverse structures by coupling multiple sequence alignment (MSA) with electron-density sampling. FLEXR-MSA generates visualizations that pinpoint low-occupancy features on the residue level and chart them across the protein surface to reveal global changes. To exemplify the utility of this tool, we probed electron densi

SUBMITTER: Stachowski TR 

PROVIDER: S-EPMC11878447 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature