缓冲器(光纤)
同质性(统计学)
热稳定性
缓冲溶液
小分子
化学
色谱法
材料科学
生物化学
有机化学
计算机科学
电信
机器学习
作者
Linda Reinhard,Hubert Mayerhofer,Arie Geerlof,Jochen Mueller‐Dieckmann,M.S. Weiss
出处
期刊:Acta crystallographica
[International Union of Crystallography]
日期:2013-01-30
卷期号:69 (2): 209-214
被引量:80
标识
DOI:10.1107/s1744309112051858
摘要
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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