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Silver Bullets • Silver Bullets Bio
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Silver Bullets • Silver Bullets Bio
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| Crystals of Beta amylase grown in Silver Bullets |
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| Mellitic acid, a Silver Bullet for Trypsin |
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Primary, secondary or orthoganol crystallization screen for biological macromolecules
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For use with soluble proteins and membrane proteins
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A methodology to uncover different crystal forms
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Optimization screening in conjunction with preliminary crystallization conditions
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ThermoFluor® assays
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Solubility, folding and stability studies
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Screens a portfolio of small molecules for their ability to establish stabilizing, intermolecular, hydrogen bonding, hydrophobic and electrostatic interactions which could promote lattice formation and crystallization
 | | | Organic salts & acids |
| | | Biologically active small molecules |
| | | Amino acids and peptides |
| | | Macromolecular digests |
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Modular screen design allows Silver Bullets to be screened against virtually any crystallization reagent
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Developed at Hampton Research
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Original & Bio Formulations
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A combinatorial library of more than 1,090 chemicals, of which more than 400 are unique
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Available in Deep Well block format
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An alternative approach to macromolecular crystallization.
The Silver Bullets formulation and methodology screens validated small molecule libraries against a few select crystallization reagents as an effective, orthogonal approach to macromolecular crystallization. The formulation offers an alternative and efficient approach that is an excellent complement to current crystallization methodologies.
Silver Bullets is a library of small molecules that have been shown to promote crystal lattice formation. X-ray diffraction analysis has demonstrated the reagents have the ability to:
• Stabilize the conformation of the protein
• Perturb the interaction of the protein with the solvent
• Participate in forming important lattice contacts
• Build the crystal lattice by forming reversible cross-links between the macromolecules in the crystal
Results with the Silver Bullets approach have been very encouraging, with more than twice as many proteins being crystallized overall as were crystallized from controls free of any small molecules.1-3 There have been frequent occasions where some exceptional result has been obtained for specific proteins, and numerous examples where new or unusual crystal forms were obtained. X-ray diffraction analysis has revealed the small molecules in the crystal lattice, involved at the centers of hydrogen bonding networks and electrostatic interaction.3-4
Silver Bullets can be used as a primary crystallization screen; as a secondary or orthogonal screen to produce crystals when traditional screens are not successful; as an optimization screen in conjunction with preliminary crystallization conditions; as a methodology to uncover different crystal forms; to promote intramolecular interactions that may stabilize a macromolecules conformation and promote crystallization.
Silver Bullets and Silver Bullets Bio can be utilized with Differential Scanning Fluorimetry (DSF, ThermoFluor) and Protein Thermal Shift assay to identify optimal ligands required for
maximizing protein crystallization success.
Silver Bullets solutions are designed for use with the Silver Bullets PEG/Tacsimate Crystallization Reagents but may also be used with other crystallization reagents.
The Silver Bullets kits are composed of 96 solutions in a single Deep Well block (Greiner 786261) HT format. Each reagent is a mixture of small molecules or macromolecular digest in 0.02 M HEPES sodium pH 6.8 buffer. Each Silver Bullets solution is supplied in a 0.25 ml volume. Each solution contains between 2 and 20 small molecules.
Silver Bullets reagents include: Organic salts and acids • Biologically active molecules
• Amino acids and peptides • Macromolecular digests
Silver Bullets Bio reagents include: Small organic molecules, organic salts, and organic acids
• Biologically active molecules, co-factors, and ligands • Amino acids, peptides, nucleotides, drugs, and carbohydrates • Biochemical pathway intermediates
The PEG/Tacsimate Crystallization Reagents are composed of 96 reagents in a single 1 ml Deep Well block.
ThermoFluor is a registered trademark of Johnson & Johnson.
Protein Thermal Shift is a trademark of Applied Biosystems.
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CAT NO |
NAME |
DESCRIPTION |
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| HR2-096 |
Silver Bullets HT |
0.25 ml, Deep Well block format |
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CAT NO |
NAME |
DESCRIPTION |
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| HR2-088 |
Silver Bullets Bio HT |
0.25 ml, Deep Well block format |
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CAT NO |
NAME |
DESCRIPTION |
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| HR2-090 |
PEG/Tacsimate pH 5.8 Crystallization Reagent |
1 ml, Deep Well block format |
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CAT NO |
NAME |
DESCRIPTION |
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| HR2-092 |
PEG/Tacsimate pH 6.8 Crystallization Reagent |
1 ml, Deep Well block format |
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CAT NO |
NAME |
DESCRIPTION |
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| HR2-094 |
PEG/Tacsimate pH 7.8 Crystallization Reagent |
1 ml, Deep Well block format |
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References
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| 1. | Searching for silver bullets: An alternative strategy for crystallizing macromolecules. Alexander McPherson and Bob Cudney. Journal of Structural Biology 156 (2006) 387-406. |
| 2. | A novel strategy for the crystallization of proteins: X-ray diffraction validation. Steven B. Larson, John S. Day, Robert Cudney, and Alexander McPherson. Acta Cryst. (2007) D63, 310-318. |
| 3. | A new crystal form of bovine pancreatic RNase A in complex with 2'-deoxyguanosine-5'-monophosphate. S. B. Larson, J. S. Day, R. Cudney and A. McPherson. Acta Cryst. (2007). F63, 728-733. |
| 4. | Development of an alternative approach to protein crystallization. McPherson, Alexander; Nguyen, Chieniang; Larson, Steven B; Day, John S; Cudney, Bob. J Struct Funct Genomics, Volume 8, Number 4, December 2007, 193-198. |
| 5. | Progress in the Development of an Alternative Approach to Macromolecular Crystallization. S. B. Larson,J. S. Day, C. Nguyen, R. Cudney, and A. McPherson. Crystal Growth & Design 2008 Volume 8, No. 8 3038-3052. |
| 6. | High-resolution structure of proteinase K cocrystallized with digalacturonic acid. S. B. Larson, J. S. Day, C. Nguyen, R. Cudney and A. McPherson. Acta Cryst. (2009). F65, 192-198. |
| 7. | Structure of pig heart citrate synthase at 1.78 Angstrom resolution. Steven B. Larson, John S. Day, Chieugiang Nguyen, Robert Cudney and Alexander McPherson. Acta Cryst. (2009). F65, 430–434. |
| 8. | Crystallization and preliminary X-ray diffraction analysis of the dimerization domain of the tumour suppressor ING4. Simone Culurgioni et al, Acta Cryst. (2010). F66, 567–570. |
| 9. | Crystallization and preliminary X-ray analysis of the chemokine-binding protein from orf virus (Poxviridae). R. M. Couñago, S. B. Fleming, A. A. Mercer and K. L. Krause. Acta Cryst. (2010). F66, 819-823. Synopsis: The morphology and diffraction behaviour of these crystals was significantly improved through the use of Silver Bullets. |
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