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Detergent Screen HT
Detergent Screen HT

Detergent Screen HT
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Detergent Screen HT
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Prevent and manipulate non-specific aggregation due to hydrophobic interactions
Kits include popular detergents used in the crystallization of membrane proteins
Ionic detergents
Non-ionic detergents
Zwitterionic detergents
Non-detergent Sulfobetaines
Synthetic lipids
Useful with soluble proteins where hydrophobic interactions limit sample solubility
Detergents are compatible with microbatch under oil crystallization, as well as vapor diffusion, free interface diffusion and dialysis
Deep Well block format
Additive screen for protein crystallization
Protein stability screen (Thermofluor with CCVJ)
Detergent Screen HT is designed to allow the rapid and convenient evaluation of a total of 96 unique detergent reagents for their ability to influence the solubility and crystallization of the sample. The screen is designed to be compatible with most popular crystallization reagents.

The detergents in the kit are capable of manipulating hydrophobic sample-sample interactions which can lead to non-specific aggregation, and prevent or interfere with sample crystallization. The detergents also perturb water structure which may play a role in sample crystallization.

Non-specific aggregation is a common deterrent to the crystallization of soluble macromolecules as well as membrane proteins. There is extensive literature demonstrating the effectiveness of including detergents in the crystallization trial towards preventing non-specific aggregation due to hydrophobic interactions and hence improving crystallization.1-7 The kits allow one to screen the most effective detergents used in crystal growth.

The Detergent Screen kit is formulated so that simple pipetting is all that is required to screen the detergents with the hanging or sitting drop vapor diffusion technique. Screens with kit are usually performed after preliminary crystallization conditions have been determined, although ab initio screens are also practical. The kit is recommended for both soluble and membrane proteins where non-specific aggregation is a suspected complication or where one simply wishes to screen detergents as an optimization variable.

The screen is suitable for hanging drop, sitting drop, microbatch, free interface diffusion and sandwich drop crystallization methodologies. Ready-to-use reagents are sterile filtered and formulated with ultra-pure Type 1 water, using the highest purity detergents and are filled under argon gas to enhance stability.

Each Detergent Screen HT kit contains 96 unique detergents. 0.25 ml of detergent solution is formulated at 10 times the reported CMC (unless otherwise noted) in sterile filtered deionized water. The Detergent Screen HT kit contains 96 solutions in a single Deep Well block.
HR2-406 Detergent Screen HT 0.25 ml, Deep Well block format
Price Quantity
1.Crystallization of membrane proteins. Edited by Hartmut Michel, CRC Press, (1991).
2.Crystallization of Nucleic Acids and Proteins: A Practical Approach. Oxford University Press, Pages 175-191 (1992).
3.McPherson, A., et al., The effects of neutral detergents on the crystallization of soluble proteins., J. Crystal Growth (1986) 76, 547-553.
4.Kuhlbrand, W., Quarterly Rev. Biophys. (1988) 21, 429.
5.Garavito, R.M., & Picot, D., Methods, A Companion to Methods in Enzymology (1990) 1, 57.
6.Garavito, R.M,. et al., J. Crystal Growth (1986) 76, 701-709. 7. Cudney, R., et al., Acta Cryst. (1994) D50, 414-423.
7.Thomas R.M. Barenda and Bauke W. Diskstra. Oils used in microbatch crystallization do not remove a detergent from the drops they cover. Acta Cryst. (2003). D59, 2345-2347.
8.Loll et al. Compatibility of detergents with the microbatch-under-oil crystallization method. Acta Cryst. (2003). D59, 114-116.
9.Overexpression, crystallization and preliminary X-ray crystallographic analysis of the ectoine hydroxylase from Sphingopyxis alaskensis. A. Hoeppner, N. Widderich, E. Bremer and S. H. J. Smits. Acta Cryst. (2014). F70, 493-496 [ doi:10.1107/S2053230X14004798 ]
10.Differential scanning fluorescence approach using a fluorescent molecular rotor to detect thermostability in proteins in surfactant-containing formulations. Ablinger et al, International Journal of Pharmaceutics 441 (2013) 255-260
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