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Open Access Green as soon as Postprint is submitted to ZB.
Optimization of protein buffer cocktails using Thermofluor.
Acta Crystallogr. F-Struct. Biol. Cryst. Commun. 69, 209-214 (2013)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
differential scanning fluorimetry; protein buffer cocktails; protein unfolding; small-molecule additives; thermal shift assay; Thermofluor
e-ISSN
2053-230X
Journal
Acta Crystallographica Section F
Quellenangaben
Volume: 69,
Issue: 2,
Pages: 209-214
Publisher
Blackwell
Publishing Place
Oxford [u.a.]
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)