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Products > Crystallization Screens > Grid Screens > Grid Screen PEG 6000
Grid Screen PEG 6000
Applications
- Primary or secondary, Polyethylene glycol 6,000 versus pH grid crystallization screen for biological macromolecules
Features
- A systematic grid screen varying Polyethylene glycol 6,000 concentration versus pH
- Samples pH 4 to 9
- Samples four concentrations of Polyethylene glycol 6,000
- Precise pH versus Polyethylene glycol 6,000 screen
- pH adjusted after salt addition; 25°Celsius
- Combine reagents between rows or columns to create expanded grid screens
Description
Grid Screen™ PEG 6000 is a preformulated reagent kit designed to provide a rapid screening method for the crystallization of biological macromolecules.
The screen is simple and practical for finding initial crystallization conditions as well as determining the solubility of a macromolecule in Polyethylene glycol 6,000 between pH 4.0 and 9.0.
Grid Screen PEG 6000 evaluates Polyethylene glycol at four concentrations (5, 10, 20, 30 %w/v) versus six pH levels (4, 5, 6, 7, 8, 9).
Grid Screen PEG 6000 consists of 24 unique reagents, each supplied as 10 milliliter in sterile, screw cap tubes. Ready-to-use reagents are sterile filtered and formulated with ultra-pure Type 1 water, using the highest purity polymer and buffers. Individual reagents are available through the Hampton Research Custom Shop.
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CAT NO
HR2-213
NAME
DESCRIPTION
10 ml, tube format
PRICE
$138.00
cart quote
Support Material(s)
HR2-213 Grid Screen PEG 6000 Documents
HR2-213 Grid Screen PEG 6000 SDS
Grid Screen PEG 6000 Formulation & Scoring Data Related Item(S)
- Individual Grid Screen PEG 6000 Reagents
References
1. Advance in Protein Chemistry Volume 41. Pages 1-33 (Patricia C. Weber). Academic Press, 1991.
2. Crystallization of nucleic acids and proteins, Edited by A. Ducruix and R. Giege, The Practical Approach Series, Oxford Univ. Press, 1992.
3. Current approaches to macromolecular crystallization. McPherson, A. Eur. J. Biochem. 189, 1-23, 1990.
4. Protein and Nucleic Acid Crystallization. Methods, A Companion to Methods in Enzymology, Academic Press, Volume 1, Number 1, August 1990.
5. A protein crystallization strategy using automated grid searches on successively finer grids. Patricia C. Weber. Methods: A Companion to Methods in Enzymology Vol. 1, No. 1, August, pp. 31-37, 1990.
6. Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase. Mayumi Igura,a Toyoyuki Ose, Takayuki Obita, Chiaki Sato, Katsumi Maenaka, Toshiya Endo, and Daisuke Kohda. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1; 61(Pt 5): 514–517.
7. Crystallization and X-ray diffraction analysis of human CLEC-2. Aleksandra A. Watson and Christopher A. O′Callaghan. ActaCryst. (2005). F 61 , 1094-1096.
Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).
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