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Proteins are dynamic molecules that exhibit a wide range of motions; often these conformational changes are important for protein function. Determining biologically relevant conformational changes, or true variability, efficiently is challenging due to the noise present in structure data. Results: In this paper we present a novel approach to elucidate conformational variability in structures solved using X-ray crystallography. We first infer an ensemble to represent the experimental data anddoi:10.1186/1748-7188-6-12 pmid:21504605 pmcid:PMC3101643 fatcat:oc45jrpfjfbafovgfuzizu72s4