HEPES sodium 
Synonyms: HEPES sodium salt, or 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid sodium salt, or N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid) sodium salt 
C₈H₁₇N₂O₄SNa 
M_r 260.29 
CAS [75277-39-3] 
EC Number 278-169-7 
MDL Number MFCD00036463 
PubChem Substance ID 24895780 
pKa 7.4-7.7 at 25°C 
Useful pH Range of HEPES sodium: 6.6-8.5

StockOptions Sodium HEPES 66 185ml

StockOptions Sodium HEPES 67 185ml

StockOptions Sodium HEPES 01 185ml

StockOptions Sodium HEPES 02 185ml

StockOptions Sodium HEPES 03 185ml

StockOptions Sodium HEPES 04 185ml

StockOptions Sodium HEPES 05 185ml

StockOptions Sodium HEPES 06 185ml

StockOptions Sodium HEPES 07 185ml

StockOptions Sodium HEPES 08 185ml

StockOptions Sodium HEPES 09 185ml

StockOptions Sodium HEPES 10 185ml

StockOptions Sodium HEPES 11 185ml

StockOptions Sodium HEPES 12 185ml

StockOptions Sodium HEPES 13 185ml

StockOptions Sodium HEPES 14 185ml

StockOptions Sodium HEPES 15 185ml

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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Dow Corning Vacuum Grease

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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The plates can be sealed using Crystal Clear Sealing Film (HR3-609), 3 inch wide Crystal Clear Sealing Tape (HR4-506) or ClearSeal Film™ (HR4-521). Corning has discontinued 3557 – special pricing and limited inventory available for this item only.

Corning 3557

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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Synonym: N-[Tris(hydroxymethyl)methyl]glycine 
(HOCH₂)₃CNHCH₂CO₂H 
M_r 179.17 
CAS Number [5704-04-1] 
Beilstein Registry Number 1937804 
EC Number 227-193-6 
MDL Number MFCD00004277 
PubChem Substance ID 24889851 
Purity ≥ 99.5% 

StockOptions Tricine 01 185ml

StockOptions Tricine 02 185ml

StockOptions Tricine 03 185ml

StockOptions Tricine 04 185ml

StockOptions Tricine 05 185ml

StockOptions Tricine 06 185ml

StockOptions Tricine 07 185ml

StockOptions Tricine 08 185ml

StockOptions Tricine 09 185ml

StockOptions Tricine 10 185ml

StockOptions Tricine 11 185ml

StockOptions Tricine 12 185ml

StockOptions Tricine 13 185ml

StockOptions Tricine 14 185ml

StockOptions Tricine 15 185ml

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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Dow Corning 7 Release Compound Grease

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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The well surfaces are treated to be hydrophilic for improved drop mixing. Both versions are compatible with 8 and 12 channel manual pipetters, automated liquid handling work stations, and imaging systems. Both versions are manufactured from an advanced polymer with high resistance to commonly used protein crystallization reagents. The advanced polymer material provides for low-background polarization and high optical clarity so protein crystals may be viewed under polarized light with minimal background interference. Low water absorption of the polymer prevents loss of protein drop volume.

The plates can be sealed using Crystal Clear Sealing Film (HR3-609), 3 inch wide Crystal Clear Sealing Tape (HR4-506) or ClearSeal Film™ (HR4-521)

CrystalEX 96 Well, Conical Bottom, Corning 3773

CrystalEX 96 Well, Conical Bottom, Corning 3773

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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1.0 M Tris (Tris titrated to indicated pH using HCl) 
Synonym: Trizma base or 2-Amino-2-(hydroxymethyl)-1,3-propanediol or THAM or Tris base or Tris(hydroxymethyl)aminomethane or Trometamol 
C₄H₁₁NO₃ 
NH₂C(CH₂OH)₃ 
M_r 121.14 
CAS Number [77-86-1] 
EC Number 201-064-4 
Beilstein Registry Number 741883 
Merck 14,9772 
RTECS TY2900000 
MDL Number MFCD00004679 
PubChem Substance ID 24889854 
Purity 99.8 – 100.1% 
pKa = 8.1 at 25°C 
Useful pH range of Tris = 7.0 – 9.0 

Insoluble Matter 0.005% max 
DNase None Detected 
RNase None Detected 
Protease None Detected 
Heavy Metals 5 ppm max 
As = 5 ppm max 
Ca = 5 ppm max 
Cu = 5 ppm max 
Fe = 5 ppm max 
Pb = 5 ppm max 
Mg = 5 ppm max 

Use StockOptions Tris kit (HR2-100) for a set of 21 Tris reagents titrated to pH 7.0 to 9.0 in 0.1 pH increments. 

StockOptions Tris 01 185ml

StockOptions Tris 02 185ml

StockOptions Tris 03 185ml

StockOptions Tris 04 185ml

StockOptions Tris 05 185ml

StockOptions Tris 06 185ml

StockOptions Tris 07 185ml

StockOptions Tris 08 185ml

StockOptions Tris 09 185ml

StockOptions Tris 10 185ml

StockOptions Tris 11 185ml

StockOptions Tris 12 185ml

StockOptions Tris 13 185ml

StockOptions Tris 14 185ml

StockOptions Tris 15 185ml

StockOptions Tris 16 185ml

StockOptions Tris 17 185ml

StockOptions Tris 18 185ml

StockOptions Tris 19 185ml

StockOptions Tris 20 185ml

StockOptions Tris 21 185ml

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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Grease Cartridge

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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The well surfaces are treated to be hydrophilic for improved drop mixing. Both versions are compatible with 8 and 12 channel manual pipetters, automated liquid handling work stations, and imaging systems. Both versions are manufactured from an advanced polymer with high resistance to commonly used protein crystallization reagents. The advanced polymer material provides for low-background polarization and high optical clarity so protein crystals may be viewed under polarized light with minimal background interference. Low water absorption of the polymer prevents loss of protein drop volume.

The plates can be sealed using Crystal Clear Sealing Film (HR3-609), 3 inch wide Crystal Clear Sealing Tape (HR4-506) or ClearSeal Film™ (HR4-521)

CrystalEX 96 Well, Flat Bottom, Corning 3785

CrystalEX 96 Well, Flat Bottom, Corning 3785

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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1.0M TRIS hydrochloride (Tris hydrochloride titrated to indicated pH using NaOH) 
Synonyms: TRIS HCl, Trizma hydrochloride, Tris(hydroxymethyl)aminomethane hydrochloride. 
NH₂C(CH₂OH)₃·HCl 
C₄H₁₁NO₃·HCl 
M_r 157.60 
[1185-53-1] 
EC No 214-684-5 
Beilstein Registry Number 3675235 
Purity > 99.0% 

Al <0.0005% 
As <0.0001% 
Ba <0.0005% 
Bi <0.0005% 
Ca <0.001% 
Cd <0.0005% 
Co <0.0005% 
Cr <0.0005% 
Cu <0.0005% 
Fe <0.0005% 
K <0.005% 
Li <0.0005% 
Mg <0.0005% 
Mn <0.0005% 
Mo <0.0005% 
Na <0.005% 
Ni <0.0005% 
Pb <0.0005% 
SO₄ <0.005% 
Sr <0.0005% 
Zn <0.0005%

Use StockOptions Tris Hydrochloride kit (HR2-237) for a set of 21 Tris hydrochloride reagents titrated to pH 7.0 to 9.0 in 0.1 pH increments. 

StockOptions Tris HCl 01 185ml

StockOptions Tris HCl 02 185ml

StockOptions Tris HCl 03 185ml

StockOptions Tris HCl 04 185ml

StockOptions Tris HCl 05 185ml

StockOptions Tris HCl 06 185ml

StockOptions Tris HCl 07 185ml

StockOptions Tris HCl 08 185ml

StockOptions Tris HCl 09 185ml

StockOptions Tris HCl 10 185ml

StockOptions Tris HCl 11 185ml

StockOptions Tris HCl 12 185ml

StockOptions Tris HCl 13 185ml

StockOptions Tris HCl 14 185ml

StockOptions Tris HCl 15 185ml

StockOptions Tris HCl 16 185ml

StockOptions Tris HCl 17 185ml

StockOptions Tris HCl 18 185ml

StockOptions Tris HCl 19 185ml

StockOptions Tris HCl 20 185ml

StockOptions Tris HCl 21 185ml

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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Sticky Pad

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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The Hampton Research Solubility and Stability Screen can evaluate protein solubility, stability and crystallization in the presence of 94 different chemical additives sampling 17 different classes of reagents plus two controls.

Protein solubility and stability are universally required in a wide range of applications, including general biochemical studies, the preparation of proteins in pharmaceuticals, structural biology and crystallization.^1-11 The preparation of a concentrated, soluble and stable protein sample can often be a difficult task as proteins often aggregate, precipitate or denature.

Thermofluor (also known as Differential Scanning Fluorimetry, DSF and Protein Thermal Shift) provides a rapid, convenient and effective means of identifying subsaturating solution conditions that may also correlate with protein heterogeneity and poor crystallization outcomes.¹²

Protein solubility and stability is affected by many different chemical factors including pH, buffer type, chemical additives and excipients. pH and buffer type are dominant protein solubility and stability variables and can be evaluated and optimized using the Hampton Research Slice pH kit HR2-070. Slice pH evaluates protein solubility, stability and crystallization versus 20 different buffers over the pH range 3.5-9.6. Chemical additives influencing protein solubility and stability can be evaluated using the Solubility & Stability Screen.

It is widely accepted that protein solubility and stability can be increased by the use of chemical additives.^5,15 Seventeen classes of reagents are sampled by the Solubility & Stability Screen and each of these classes has been reported as important in improving sample solubility and stability.^2-11

The Solubility & Stability Screen is a set of 94 high purity reagents formulated in high purity water (NCCLS/ASTM Type 1+) at 25°C and are 0.22 micron sterile filtered. The 94 solubility and stability reagents are formulated at 2 to 10 times their recommended working concentration. The remaining two reagents are water and a negative (TCA) control. A water control demonstrates the effect of diluting sample as well as sample buffer concentration. TCA, the negative control, demonstrates total sample precipitation, loss of sample solubility and loss of sample stability. The effects of the Solubility & Stability reagents can be compared with this negative control to assist in the identification of reagents promoting sample solubility and stability. 500 microliters of each reagent is supplied in a sterile 96 well polypropylene Deep Well block. The Solubility & Stability Screen reagents are compatible with the sitting or hanging drop vapor diffusion, microbatch, free interface diffusion, sandwich drop vapor diffusion, and dialysis crystallization methods utilizing water soluble reagents.

Solubility & Stability Screen

1. Preparation and analysis of protein crystals. Alexander McPherson. 1982 John Wiley and Sons, Inc.

2. A straight-forward method of optimizing protein solubility for NMR. Peter W.A. Howe, Journal of Biomolecular NMR 30: 283-286, 2004.

3. Rapid determination of protein solubility and stability conditions for NMR studies using incomplete factorial design. Demene, H. et al. Journal of Biomolecular NMR (2006) 34: 137-151.

4. Dissolution of protein aggregation by small amine compounds. Takagai et al. Science and Technology of Advanced Materials 4 (2003) 55-59.

5. Detection and prevention of protein aggregation before, during, and after purification. Sarah E. Bondos and Alicia Bicknell. Analytical Biochemistry 316 (2003) 223-231.

6. Ionic liquid 1-butyl-3-methyl imidazolium tetrafluoroborate for shotgun membrane proteomics. Sun et al. Anal Bioanal Chem (2010) DOI 10.1007/s00216-010-4381-5.

7. Stabilization of proteins by low molecular weight multi-ions. Middaugh et al. Journal of Pharmaceutical Sciences, Vol. 91, No. 10, October 2002.

8. Inhibition of aggregation side reactions during in vitro protein folding. Eliana De Bernardez Clark, Elisabeth Schwarz, Rainer Rudolph. Methods in Enzymology Volume 309 page 228 (1991).

9. Refolding a glutamine synthetase truncation mutant in vitro: Identifying superior conditions using a combination of chaperonins and osmolytes. Paul A. Voziyan, Lalita Jadhav, Mark T. Fisher. Journal of Pharmaceutical Science Volume 89 page 1036 (2000).

10. Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses. Goloubinoff et al. J. Biol. Chem., Vol. 276, Issue 43, 39586-39591, October 26, 2001.

11. Effect of additives on protein aggregation. Shiraki et al. Current Pharmaceutical Biotechnology, 2009, 10, 400-407.

12. A thermal stability assay can help to estimate the crystallization likelihood of biological samples. Marquez et al. Acta Cryst. (2011). D67, 915-919.

13. The combined use of the Thermofluor assay and ThermoQ analytical software for the determination of protein stability and buffer optimization as an aid in protein crystallization. Kevin Phillips and Andres Hernandez de la Pena. Current Protocols in Molecular Biology 10.28.1-10.28.15 April 2011.

14. Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin. Romao et al. Protein Expression and Purification 81 (2012) 193-200.

15. Optimization of protein solubility and stability for protein nuclear magnetic resonance. Bagby S, Tong KI, Ikura, M. Methods Enzymol. 2001;339:20-41.

16. High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery. Pantoliano et al, Journal of Biomolecular Screening, Volume 6, Number 6, 2001.

17. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Ericsson, U.B. et al, Anal Biochem. 2006 Oct 15;357(2):289-98. Epub 2006 Aug 10.

18. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Vedadi, M. et al, Proc Natl Acad Sci U S A. 2006 Oct 24;103(43):15835-40. Epub 2006 Oct 11.

19. Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes. J. Kopec, G. Schneider. Journal of Structural Biology 175 (2011) 216-223.

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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Crystal Clear Sealing Film

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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The preparation of a concentrated, soluble and stable protein sample can often be a difficult task as proteins often aggregate, precipitate or denature.

Protein solubility and stability is affected by many different chemical factors including pH, buffer type, ionic strength and protein specific additives. pH, buffer type and ionic strength are dominant protein solubility and stability variables that can be evaluated and optimized using the Solubility and Stability Screen 2.

No clear correlation between intrinsic properties of proteins and solubility and stability exist, so systematic screening can help to identify optimal sample buffer conditions. Protein solubility and stability screening, performed using Dynamic Light Scattering and ThermoFluor assays together with the Solubility and Stability Screens and Slice pH can be an extremely data rich, informative, efficient, and cost-effective method for the identification of sample buffer conditions that maximally stabilize a protein for protein purification, formulation, crystallization, and functional characterization.

Dynamic Light Scattering (DLS) is an established technique for determining the size, monodispersity and polydispersity of proteins in solution. DLS with a plate reader allows a multitude of buffers, pH, ionic strength, protein specific additives and temperature to be screened. Combining Solubility & Stability Screens with DLS, particle size and size distribution, unfolding of proteins, crystallizability, thermal stability, aggregation and solubility behavior and be evaluated in a high throughput format.

The ThermoFluor assay is an established technique for assessing protein thermostability in solution. ThermoFluor allows systematic assessment of many reagents simultaneously, uses only small a small amount of protein, and is accessible to anyone with a real-time PCR instrument.

Once an optimal buffer, pH and ionic strength is identified, the sample can be exchanged into the new optimal buffer. Using this optimized sample, further ThermoFluor assays with the Solubility & Stability Screen, Silver Bullets, Silver Bullets Bio and Additive Screen can be performed to identify protein specific additives that further promote solubility and stability of the protein.

ThermoFluor^® is a registered trademark of Johnson & Johnson.

Protein Thermal Shift is a trademark of ThermoFisher.

Sypro^® is a registered trademark of ThermoFisher.

Solubility & Stability Screen 2

1. A thermal stability assay can help to estimate the crystallization likelihood of biological samples. Marquez et al. Acta Cryst. (2011). D67, 915-919.

2. The combined use of the ThermoFluor assay and ThermoQ analytical software for the determination of protein stability and buffer optimization as an aid in protein crystallization. Kevin Phillips and Andres Hernandez de la Pena. Current Protocols in Molecular Biology 10.28.1-10.28.15 April 2011.

3. Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin. Romao et al. Protein Expression and Purification 81 (2012) 193-200.

4. Optimization of protein solubility and stability for protein nuclear magnetic resonance. Bagby S, Tong KI, Ikura, M. Methods Enzymol. 2001;339:20-41.

5. High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery. Pantoliano et al, Journal of Biomolecular Screening, Volume 6, Number 6, 2001.

6. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Ericsson, U.B. et al, Anal Biochem. 2006 Oct 15;357(2):289-98. Epub 2006 Aug 10.

7. Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes. J. Kopec, G. Schneider. Journal of Structural Biology 175 (2011) 216-223.

8. Enhancing recombinant protein quality and yield by protein stability profiling. Mezzasalma TM, Kranz JK, Chan W, Struble GT, Schalk-Hihi C, Deckman IC, Springer BA, Todd MJ. J Biomol Screen. 2007 Apr;12(3):418-28.

9. Optimization of protein purification and characterization using ThermoFluor screens. Boivin S, Kozak S, Meijers R. Protein Expr Purif. 2013 Oct;91(2):192-206. doi: 10.1016/j.pep.2013.08.002. Epub 2013 Aug 12.

10. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Frank H Niesen, Helena Berglund & Masoud Vedadi. Nat Protoc. 2007;2(9):2212-21.

11. Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies. Ferre-D′Amare AR1, Burley SK. Structure. 1994 May 15;2(5):357-9.

12. Crystallizing proteins – a rational approach? D′Arcy A. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):469-71.

13. Protein Crystallization. Techniques, Strategies, and Tips. A Laboratory Manual. Edited by Terese M. Bergfors. International University Line. 1999; 27-38.

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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Catalog number HR3-511 is a 1.88 inch (48 mm) wide, 3 mil tape on a 43.7 yard (40 M) roll with a 1.5 inch core and is supplied with a green dispenser / cutter.

Catalog number HR4-511 is a 1.88 inch wide, 3 mil tape on a 109.3 yard roll with a 3 inch core and no dispenser / cutter.

Two strips of the HR3-511 or HR4-511 will seal a Corning, Cryschem, CrystalClear Strip, Greiner, Intelliplate, Linbro, Swissci (MRC), VDX and VDXm plate.

Catalog number HR4-506 is a 3 inch wide, 3 mil tape on a 54.86 yard roll with a 3 inch core and no dispenser / cutter.

One strip of the HR4-506 will seal a Corning, Cryschem M, CrystalClear Strip, Greiner, Intelliplate, Swissci (MRC) and VDXm plate.

Crystal Clear Mini Sealing Tape HR4-508 is a 0.75 inch (19 mm) wide, 3 mil tape on a 650 inch (16.5 M) roll and is supplied with a clear dispenser / cutter. The tape is useful for resealing or patching wells after mounting crystals. The tape is also wide enough to seal a single row of a Cryschem S or Cryschem M plate.

See chart for tape and plate compatibility.

1.88 inch wide Crystal Clear Sealing Tape

1.88 inch wide Crystal Clear Sealing Tape

3 inch wide Crystal Clear Sealing Tape

0.75 inch wide Crystal Clear Mini Sealing Tape

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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pH is an effective solubility, stability and crystallization variable because most proteins demonstrate pH dependent solubility minima and will solubilize, precipitate, or crystallize at particular pH values or in the presence of specific buffers. The solubility minima may correspond with the isoelectric point (pI) of the protein, but this is not always the case. The solubility minima and maxima is often complex and may depend on other chemical and physical variables in the crystallization experiment.

Using Slice pH one isolates pH, buffer type and relative supersaturation from other chemical and physical variables and to screen the effect that pH and buffer type have on the solubility, stability, homogeneity, monodispersity and crystallization of the sample. Varying the pH can alter the protonation state and charge of amino acid residues in the protein, generating different species of the protein for solubility and crystallization screening. The change in pH can have a dramatic effect on inter and intramolecular contacts in the protein and can manipulate how the protein interacts with itself, the surrounding solvent and chemicals in the drop. By screening buffer type and pH in an environment of increasing relative supersaturation, Slice pH simultaneously delivers as a solubility and a crystallization screen for proteins. After the screen, and once the appropriate sample buffer and pH are identified, the sample can be exchanged into the identified buffer and pH for optimal solubility and stability. From this point, the sample in the optimized buffer reagent can be used for crystallization trials or other assays. Further, crystallization screening and optimization experiments may be more appropriately focused on the optimal pH range and buffer type.

The Slice pH kit contains 500 microliters of 96 reagents in a V-Bottom (conical bottom) 96 Deep Well polypropylene microplate, user guide, formulations and a sealing film.

Slice pH

1. Preparation and analysis of protein crystals. Alexander McPherson. 1982 John Wiley and Sons, Inc.

2. Increasing the size of microcrystals by fine sampling of pH limits. Alexander McPherson. J. Appl. Cryst. (1995). 28, 362-365.

3. Protein crystallization techniques, strategies and tips. Edited by Terese Bergfors. 1999. International University Line.

4. Crystallization of Biological Macromolecules. Alexander McPherson. 1991. Cold Spring Harbor Laboratory Press.

5. Current approaches to macromolecular crystallization (review). Alexander McPherson. Eur. J. Biochem. 189, 1-23 (1990).

6. Protein Isoelectric Point as a Predictor for Increased Crystallization screening efficiency. Katherine A. Kantardjieff and Bernhard Rupp. Bioinformatics (2004) 20.

7. A protein crystallization strategy using automated grid searches on successively finer grid screens. Patricia C. Weber. Methods: A Companion to Methods in Enzymology. Vol. 1, No. 1, August, pp. 31-37, 1990.

8. Two approaches to the rapid screening of crystallization conditions. Alexander McPherson. Journal of Crystal Growth 122 (1992) 161-167.

9. Optimization of buffer solutions for protein crystallization. R. A. Gosavi, T. C. Mueser and C. A. Schall. Acta Cryst. (2008). D64, 506-514.

10. Buffer Solutions The Basics. R.J. Beynon and J.S. Easterby. 1996. IRL Press.

11. Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin. Santos SP, Bandeiras TM, Pinto AF, Teixeira M, Carrondo MA, Romão CV. Protein Expr Purif. 2012 Feb;81(2):193-200. doi: 10.1016/j.pep.2011.10.001. Epub 2011 Oct 24.

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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