ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Optimization of protein buffer cocktails using Thermofluor.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 86 citations in OpenAlex.
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- Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O.Journal of visualized experiments : JoVE · 2024Article
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- Screening of Buffers and Additives for Protein Stabilization by Thermal Shift Assay: A Practical Approach.Methods in molecular biology (Clifton, N.J.) · 2023Article
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- Thermofluor-Based Analysis of Protein Integrity and Ligand Interactions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Ionic Liquids as Protein Crystallization Additives.Crystals · 2021Article
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- Development of 48-condition buffer screen for protein stability assessment.European biophysics journal : EBJ · 2021Article
- Structural Characterization of Glycerol Kinase from the Thermophilic FungusInternational journal of molecular sciences · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The stability and homogeneity of a protein sample is strongly influenced by the composition of the buffer that the protein is in. A quick and easy approach to identify a buffer composition which increases the stability and possibly the conformational homogeneity of a protein sample is the fluorescence-based thermal-shift assay (Thermofluor). Here, a novel 96-condition screen for Thermofluor experiments is presented which consists of buffer and additive parts. The buffer screen comprises 23 different buffers and the additive screen includes small-molecule additives such as salts and nucleotide analogues. The utilization of small-molecule components which increase the thermal stability of a protein sample frequently results in a protein preparation of higher quality and quantity and ultimately also increases the chances of the protein crystallizing.
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