Dialysis Buttons are injection molded from polystyrene, and are the size of a small button. The sample is placed in this chamber so as to create a slight dome of liquid at the top of the button. A dialysis membrane is placed over the top of the button/sample and is held in place with an O-ring. The O-ring is held in place by a groove in the Dialysis Button. Dialysis Buttons are supplied with O-rings. The 5 µl to 100 µl sized dialysis buttons have an approximate overall height of 6 mm, an approximate outside diameter of 10 mm without an O-ring in place, and an approximate diameter of 12 mm with an O-ring in place. The 200 µl and 350 µl sized dialysis buttons have an approximate overall height of 8 mm, an approximate outside diameter of 15 mm without an O-ring in place, and an approximate diameter of 17 mm with an O-ring in place. Each package of dialysis buttons includes a plastic golf tee shaped applicator to assist with applying a dialysis membrane to the button and securing with the supplied o-ring.

Dialysis Buttons Sampler

5 µl Dialysis Button

10 µl Dialysis Button

15 µl Dialysis Button

20 µl Dialysis Button

50 µl Dialysis Button

100 µl Dialysis Button

200 µl Dialysis Button

350 µl Dialysis Button

1. McPherson, A., Preparation and Analysis of Protein Crystals, Krieger Publishing, 88-91 (1992).

2. Durcruix, A, and Giege, R., Crystallization of Nucleic Acids and Proteins, A Practical Approach, Oxford University Press, 78-82 (1992).

3. Zeppenzauer, M., et al., Acta Chem Scan (1967) 21, 1009.

4. Structure of the membrane domain of respiratory complex I. Efremov RG, Sazanov LA. Nature. 2011 Aug 7;476(7361):414-20. doi: 10.1038/nature10330.

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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Santovac Cryo Oil offers low viscosity, incredibly low vapor pressure, low surface tension, excellent chemical inertness and excellent thermal stability.

Dip the mounted crystal into the oil to displace surface water. Or add a small amount of Santovac to the crystallization drop before mounting the crystal. After adding the Santovac, mount the crystal using a Mounted Cryoloop. Withdraw the mounted crystal from the drop and the Santovac will coat the mounted crystal. Cryogenically cool the mounted crystal.

Santovac (Santovac 5) is a five ring polyphenyl ether (PPE) with very low vapor pressure and low reactivity. The oil is highly resistant to oxidation. The only elements in the pure polyphenyl ether are oxygen, hydrogen and carbon.

The fluid is chemically stable, non-corrosive, safe and non-toxic at normal operating temperatures.

Santovac is not miscible with water, paraffin oil, silicon oil, alkanes, or Parabar 10312 (Paratone). Santovac is miscible with acetone. Shelf life 5 years.

Santovac^® is a trademark of Santovac^® Fluids.

Santovac Cryo Oil

1. Structure of the ‘open’ form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 Å resolution from crystal grown following enzyme turnover. C.E. Nichols, A.R. Hawkins and D.K. Stammersa. Acta Crystallographic Section D, Volume 60, Part 5, Pages 971-973, May 2004.

2. Crystal Structure of the Caspase Activator Human Granzyme B, a Proteinase Highly Specific for an Asp-P1 Residue. E. Estebanez-Perpina et al. Biol. Chem., Vol. 381, pp. 1203-1214, December 2000.

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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Dialysis Membrane Discs

Dialysis Membrane Discs

Dialysis Membrane Discs

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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Formulated from TMAO dihydrate in Type 1 lab water (deionized) and sterile filtered (0.22 micron)

Synonyms: TMANO, TMAO
(CH₃)₃NO•2H₂O
C₃H₉NO•2H₂O
M_r 111.14
CAS Number [62637-93-8]
EC Number 214-675-6
Beilstein Registry Number 4(4)144
Merck 14,9711
RTECS YH2850000
Purity ≥ 98.0%

Measured pH range: 9.2 – 10.6 at 25°C
Measured Conductivity Range: 5.6 – 96.6 µS/cm at 25°C
Measured Refractive Index Range: 1.37660 – 1.37804 at 20°C

When using TMAO as a cryoprotectant, try soaking the crystals in 4.0 M TMAO for 10 seconds and then cryo cool directly in the cryo stream.

4.0 M TMAO

1. Trimethylamine N-oxide as a versatile cryoprotective agent in macromolecular crystallography. Christoph Mueller-Dieckmann, Brice Kauffmann and Manfred S. Weiss. J. Appl. Cryst. (2011). 44, 433–436 doi:10.1107/S0021889811000045.

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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Synonyms: N-(2-Acetamido)iminodiacetic acid;
N-(Carbamoylmethyl)iminodiacetic acid
C₆H₁₀N₂O₅
H₂NCOCH₂N(CH₂CO₂H)₂
M_r 190.16
CAS Number [26239-55-4]
EC Number 247-530-0
Beilstein Registry Number 1787181
Merck 14,147
Purity ≥ 99.0%
MDL Number MFCD00008031
PubChem Substance ID 24845005
pKa = 6.6 at 25°Celsius

Useful pH range of ADA is 5.6 – 7.5

Titrate HR2-507 to the desired pH using NaOH
HR2-817 is titrated to pH 6.5 using NaOH

HR2-507 measured Conductivity range: 23.6 – 28.6 mS/cm at 25°C
HR2-507 measured Refractive Index range: 1.35009 – 1.35044 at 20°C

HR2-817 measured Conductivity range: 42.2 – 50.4 mS/cm at 25°C
HR2-817 measured Refractive Index range: 1.36787 – 1.36913 at 20°C

ADA buffer is used in the Hampton Research MembFac crystallization kit.

Total Impurities Insoluble matter, passes filter test
Al  ≤0.0005%
As ≤0.00001%
Ba ≤0.0005%
Bi  ≤0.0005%
Ca ≤0.001%
Cd ≤0.0005%
Cl  ≤0.1%
Co ≤0.0005%
Cr  ≤0.0005%
Cu ≤0.0005%
Fe  ≤0.0005%
K   ≤0.005%
Mg ≤0.0005%
Mn ≤0.0005%
Mo ≤0.0005%
Na ≤0.05%
Ni  ≤0.0005%
Pb  ≤0.0005%
SO₄ ≤0.005%
Sr  ≤0.0005%
Zn  ≤0.0005%

0.5 M ADA

1.0 M ADA pH 6.5

1. Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Arni, RK; Padmanabhan, K; Padmanabhan, KP; Wu, TP; Tulinsky, A. Biochemistry 32, 4727- 4737, 1993.

2. Structures of Three Crystals Forms of the Sweet Protein Thaumatin. Ko, TP; Day, J; Greenwood, A; McPherson, A. Acta Crystallogr D 50, 813- 825, 1994.

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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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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Synonyms: Glacial acetic acid
CAS Number [64-19-7]
CH₃CO₂H
M_r 60.05
Beilstein Registry Number 506007
EC Number 200-580-7
MDL number MFCD00036152
PubChem Substance ID 24859247

See the pdf Using Volatile Buffers for a novel crystallization methodology using acetic acid and ammonium hydroxide to adjust drop pH and induce crystallization.

5.2 M Acetic acid

1. Preparation and analysis of protein crystals. Alexander McPherson, 1982, John Wiley and Sons, Inc., printed by Krieger Publishing. Chapter 4, Crystallization.

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

3. Crystallization and preliminary X-ray diffraction studies of the engrailed homeodomain and of an engrailed homeodomain/DNA complex. Liu et al, Biochemical and Biophysical Research Communications, Vol. 171, No. 1, 1990, pages 257-259.

4. Changes of pH during Biomacromolecule Crystallization by Vapor Diffusion using Ammonium Sulfate as the Precipitant. Mikol et al, J. Appl. Cryst. (1989). 22, 155-161.

5. A Double Cell for Controlling Nucleation and Growth of Protein Crystals. Maria Przybylska, J. Appl. Cryst. (1989). 22, 115-118

6. Crystallization of butyrate kinase 2 from Thermotoga maritima mediated by vapor diffusion of acetic acid. Diao et al, Acta Cryst. (2003). D59, 1100±1102.

7. The preparation and crystallization of Fab fragments of a family of mouse esterolytic catalytic antibodies and their complexes with a transition-state analogue. Muranova et al, Acta Cryst. (2001). D57, 1192±1195

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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•Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process, Kim D. Collins.

•Effects of naturally occurring osmolytes on protein stability and solubility; issues important in protein crystallization, D.W. Bolen.

•Practical aspects of using the microbatch method in screening conditions for protein crystallization, Allan D’Arcy, Aengus Mac Sweeney, and Alexander Haber.

•Automated systems for protein crystallization, Joel Bard, Kimberly Ercolani, Kristine Svenson, Andrea Olland, and Will Somers.

•Lipidic cubic phases as matrices for membrane protein crystallization, Peter Nollert.

•The use of recombinant and molecular engineering in protein crystallization, Zygmunt Derewenda.

•A pedestrian guide to membrane protein crystallization, Michael Wiener.

•Crystallization data mining in structural genomics: using positive and negative results to optimize protein crystallization screens, Rebecca Page and Raymond C. Stevens.

•Predictive models for protein crystallization, Bernhard Rupp and Junwen Wang.

•Crystallization of RNA and RNA-protein complexes, Ailong Ke and Jennifer A. Doudna.

•Macromolecular cryocrystallography – methods for cooling and mounting protein crystals are cryogenic temperatures, J.W. Pflugrath

Macromolecular Crystallization

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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Synonyms: Ammonia aqueous, Ammonia water
CAS Number [1336-21-6]
NH₄OH
M_r 35.05
Beilstein Registry Number 3587154
EC Number 215-647-6
MDL Number MFCD00066650

See the pdf Using Volatile Buffers for a novel crystallization methodology using acetic acid and ammonium hydroxide to adjust drop pH and induce crystallization.

5.2 M Ammonium hydroxide

1. Preparation and analysis of protein crystals. Alexander McPherson, 1982, John Wiley and Sons, Inc., printed by Krieger Publishing. Chapter 4, Crystallization.

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

3. Crystallization and preliminary X-ray diffraction studies of the engrailed homeodomain and of an engrailed homeodomain/DNA complex. Liu et al, Biochemical and Biophysical Research Communications, Vol. 171, No. 1, 1990, pages 257-259.

4. Changes of pH during Biomacromolecule Crystallization by Vapor Diffusion using Ammonium Sulfate as the Precipitant. Mikol et al, J. Appl. Cryst. (1989). 22, 155-161.

5. A Double Cell for Controlling Nucleation and Growth of Protein Crystals. Maria Przybylska, J. Appl. Cryst. (1989). 22, 115-118.

6. Crystallization of butyrate kinase 2 from Thermotoga maritima mediated by vapor diffusion of acetic acid. Diao et al, Acta Cryst. (2003). D59, 1100±1102.

7. The preparation and crystallization of Fab fragments of a family of mouse esterolytic catalytic antibodies and their complexes with a transition-state analogue. Muranova et al, Acta Cryst. (2001). D57, 1192±1195.

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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Journal of Structural Biology

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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