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Reinhard, L.* ; Mayerhofer, H.* ; Geerlof, A. ; Müller-Dieckmann, J.* ; Weiss, M.S.*

Optimization of protein buffer cocktails using Thermofluor.

Acta Crystallogr. F-Struct. Biol. Cryst. Commun. 69, 209-214 (2013)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter differential scanning fluorimetry; protein buffer cocktails; protein unfolding; small-molecule additives; thermal shift assay; Thermofluor
Sprache englisch
Veröffentlichungsjahr 2013
HGF-Berichtsjahr 2013
e-ISSN 2053-230X
Zeitschrift Acta Crystallographica Section F
Quellenangaben Band: 69, Heft: 2, Seiten: 209-214 Artikelnummer: , Supplement: ,
Verlag Blackwell
Verlagsort Oxford [u.a.]
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503000-003
PubMed ID 23385769
DOI 10.1107/S1744309112051858
Scopus ID 84873590925
Erfassungsdatum 2013-08-01
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