Crystallization refers to the formation of solid crystals from a homogeneous solution. It is essentially a solid-liquid separation technique and a very important one at that.
Example of Crystallization
1. Water freezing
2. Removing sucrose from beet solutions
3. Removing KCl from an aqueous solution
Crystals are grown in many shapes, which are dependent upon downstream processing or final product requirements. Crystal shapes can include cubic, tetragonal, orthorhombic, hexagonal, monoclinic, triclinic, and trigonal. In order for crystallization to take place a solution must be "supersaturated".
Supersaturation refers to a state in which the liquid (solvent) contains more dissolved solids (solute) than can ordinarily be accomodated at that temperature.
As with any separation method, equilibrium plays an important role. Below is a general solubility curve for a solid that forms hydrate (a compound that has one or more water molecules attached) as it cools.
Reference 2 below
Crystallization
Study Questions/Answers from the Handbook for Organic Chemistry Lab
Crystallization is a technique which chemists use to purify solid compounds. It is one of the fundamental procedures each chemist must master to become proficient in the laboratory. Crystallization is based on the principles of solubility: compounds (solutes) tend to be more soluble in hot liquids (solvents) than they are in cold liquids. If a saturated hot solution is allowed to cool, the solute is no longer soluble in the solvent and forms crystals of pure compound. Impurities are excluded from the growing crystals and the pure solid crystals can be separated from the dissolved impurities by filtration.
This simplified scientific description of crystallization does not give a realistic picture of how the process is accomplished in the laboratory. Rather, successful crystallization relies on a blend of science and art; its success depends more on experimentation, observation, imagination, and skill than on mathematical and physical predictions. Understanding the process of crystallization in itself will not make a student a master crystallizer, rather, this understanding must be combined with laboratory practice to gain proficiency in this technique.
How to do a crystallization
To crystallize an impure, solid compound, add just enough hot solvent is added to it to completely dissolve it. The flask then contains a hot solution, in which solute molecules – both the desired compound and impurities – move freely among the hot solvent molecules. As the solution cools, the solvent can no longer “hold” all of the solute molecules, and they begin to leave the solution and form solid crystals. During this cooling, each solute molecule in turn approaches a growing crystal and rests on the crystal surface. If the geometry of the molecule fits that of the crystal, it will be more likely to remain on the crystal than it is to go back into the solution. Therefore, each growing crystal consists of only one type of molecule, the solute. After the solution has come to room temperature, it is carefully set in an ice bath to complete the crystallization process. The chilled solution is then filtered to isolate the pure crystals and the crystals are rinsed with chilled solvent.
Detailed photos from start to finish.
2007-01-18 11:02:11
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answer #1
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answered by The Answer Man 5
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What Does Crystallization Mean and How is it Performed?
Crystallization of biological macromolecules is done using a solution of the material in some solvent, usually from a super-saturated solution of the substance in water. The process we shall discuss here, i.e. the crystallization of proteins from their aqueous solutions, are entirely analogous to those which govern the crystallization of small molecules such as sugar or salt. In each case the solution is allowed to become supersaturated with solute (protein), and at some point, crystals of the solute apperar and grow in size. We should define supersaturation. If we have a cup of water, we may dissolve sugar in it up to a point at which no more sugar will dissolve, no matter how much we stir the mixture. We then have a solution of sugar in water, in contact with solid sugar. This system is said to be in equilibrium and neither crystallization nor dissolution takes place. This solution is said to be saturated, and at a given temperature the concentration of sugar in water is fixed. Normally, and as certainly the case for sugar, a saturated solution at say 50 degrees Celcius contains much more sugar in solution than does the same volume of solution saturated at 20 degrees Celcius. What happens then if we cool a solution of sugar saturated at 50 degrees Celcius? Usually at first nothing happens. There may be no crystallization even though the solution is cooled to 40 or 30 degrees Celcius, even though we know there is now too much sugar in the solution for it to be stable. Such a solution is called supersaturated. At some point, crystals are able to form themselves upon some microscopic nucleus, and crystallization can recur very rapidly.
Proteins differ from small molecules only in the degree of supersaturation which is required to induce crystallization or to allow a useful rate of crystallization. If we have a saturated solution of a protein, we may increase its supersaturation in several ways: 1) cool it down as discussed above, 2) allow the water to evaporate, 3) add an ionic solute, e.g. salt, and 4) varying the pH. Using evaporation to form protein crystals is much like that observed when working with salt or sugar. As the water evaporates the solute (protein) starts to form crystals when the supersaturation reaches a point that the amount of water available can no longer support the high concentrations of protein.
The picture on the left shows a setup for a protein screening in what is called a Limbro box. This is used by researchers to vary the conditions in each of the wells in order to determine the optimal conditions for growing crystals. For example, a researcher may vary protein concentrations from top to bottom and pH from left to right. Because different pH levels (how acidic or basic a solution is) change the structural attractions of the amino acids that make up proteins, changes in pH can also cause a protein to crystallize. Some experiments may decide to keep pH constant, at which case, they use a buffer to keep the pH constant.
Using an ionic solute such as salt creates another problem. Ionic mateials, such as sodium chloride, or common salt, dissolve readily in water. Because of the strong electric field around these ions, Na+ and Cl-, a large number of water molecules are loosely bound around the ions in a sphere of hydration. This is because the water molecule itself is an electric dipole, with one end slightly positively charged and the other end degatively charged. The net effect of adding salt to a protein solution is to reduce the amount of water which is free to keep the protein molecules in solution. Thus, the degree of supersaturation of the protein solution is effectively increased, and crystallization becomes more likely.
Above are crystals that were grown in a limbro box using variations is protein concentration and pH. The crystals above are of lysozyme, a protein located in the tear ducts of humans and in eggs of other animals. Put your curser over each of the pictures to learn more about the formation of these crystals.
http://crystal.uah.edu/~carter/protein/crystal.htm
Crystallization is a technique which chemists use to purify solid compounds. It is one of the fundamental procedures each chemist must master to become proficient in the laboratory. Crystallization is based on the principles of solubility: compounds (solutes) tend to be more soluble in hot liquids (solvents) than they are in cold liquids. If a saturated hot solution is allowed to cool, the solute is no longer soluble in the solvent and forms crystals of pure compound. Impurities are excluded from the growing crystals and the pure solid crystals can be separated from the dissolved impurities by filtration.
This simplified scientific description of crystallization does not give a realistic picture of how the process is accomplished in the laboratory. Rather, successful crystallization relies on a blend of science and art; its success depends more on experimentation, observation, imagination, and skill than on mathematical and physical predictions. Understanding the process of crystallization in itself will not make a student a master crystallizer, rather, this understanding must be combined with laboratory practice to gain proficiency in this technique.
http://orgchem.colorado.edu/hndbksupport/cryst/cryst.html
http://orgchem.colorado.edu/hndbksupport/cryst/crystdiag.html
Crystal Formation
Crystallization is the transition from the liquid to the solid state and occurs in two stages:
1. Nucleus formation
2. Crystal growth
Atomic motion in the liquid state of a metal is almost completely disordered. Although the atoms in the liquid state do not have any definite arrangement, it is possible that some atoms at any given instant are in positions exactly corresponding to the space lattice they assume when solidified. As the energy in the liquid system decreases, the movement of the atoms decreases and the probability increases for the arrangement of a number of atoms into a characteristic lattice for that material. The energy level at which these isolated lattices form is called the freezing point.
(a)
(b)
(c)
(d)
Figure 1. Mechanism of solidification (square grids represent the unit cells)
(a) Nucleus formation
(b), (c) Growth of the crystallites
(d) Grain boundaries
Now consider a pure metal at its freezing point where both the liquid and solid states are at the same temperature. The kinetic energy of the atoms in the liquid and the solid must be the same, but there is a significant difference in potential energy. Kinetic energy is related to the speed at which the atoms move and is strictly a function of temperature. The higher the temperature, the more active are the atoms and the greater is their kinetic energy. Potential energy, on the other hand, is related to the distance between atoms. The greater the average distance between the atoms, the greater is their potential energy. The atoms in the solid are much closer together, so that solidification occurs with a release of energy. This difference in potential energy between the liquid and solid states is known as the latent heat of fusion.
When the temperature of the liquid metal has dropped sufficiently below its freezing point, stable aggregates or nuclei appear spontaneously at various points in the liquid. These nuclei, which have now solidified, act as centers for further crystallization. As cooling continues, more atoms tend to freeze, and they may attach themselves to already existing nuclei or form new nuclei of their own. Each nucleus grows by the attraction of atoms from the liquid into its space lattice. Crystal growth continues in three dimensions, the atoms attaching themselves in certain preferred directions, usually along the axes of a crystal. This gives rise to a characteristic treelike structure which is called dendrite.
Figure 2. Process of crystallization by nucleation and dendritic growth.
Since each nucleus is formed by chance, the crystal axes are pointed at random and the dendrites will grow in different directions in each crystal. Finally, as the amount of liquid decreases, the gaps between the arms of the dendrite will be filled and the growth of the dendrite will be mutually obstructed by that of its neighbors. This leads to a very irregular external shape. The crystals found in all commercial metals are commonly called grains because of this variation in external shape. The area along which crystals meet, known as the grain boundary, is a region of mismatch. The boundaries are formed by materials that are not part of a lattice, such as impurities, which do not show a specific grain pattern. This leads to a noncrystalline (amorphous) structure at the grain boundary with the atoms irregularly spaced. Since the last liquid to solidify is generally along the grain boundaries, there tends to be a higher concentration of impurity atoms in that area.
Figure 3. Grain Boundary
Figure 4. Formation of dendrites in a molten metal.
Figure 5. Dendrites observed at a magnification of 250
http://www.tech.farmingdale.edu/depts/met/met205/crystallization.html
Crystallization
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Introduction
Applications
References
Product List
Introduction
The elucidation of a macromolecular structure to the atomic level by X-ray or neutron diffraction analysis requires the molecule to be available in the form of relatively large single crystals. Many soluble proteins, membrane proteins, nucleic acids and nucleoprotein complexes have been obtained in a crystalline form suitable for crystallographic investigation [1-12].
If a solution of a biopolymer is brought to supersaturation, the biopolymer may form an amorphous precipitate or crystals suitable for X-ray diffraction analysis. Sometimes anything between these two extremes can be observed. Parameters such as pH and temperature, the chemical composition of the crystallization solution, and the rate of supersaturation decide whether an amorphous precipitate or crystals are formed.
Supersaturation is often achieved by increasing the concentration of precipitating agent in the crystallization solution. Auxiliary substances may decide whether supersaturation leads to crystallization, or may improve crystallization.
Larger structures, such as the purple membrane [13] or ribosomal particies [14] may be grown into ordered two-dimensional structures in vitro. These structures can be investigated by optical or electron diffraction and subsequent three-dimensional image reconstruction, with 7 Å resolution.
Applications
1. Precipitation Reagents
The general mode of action of a precipitation reagent is the binding of water. This results in a water content insufficient to maintain the hydration of the biopolymers (or for complete protection of the biopolymers from one another). Salts, organic solvents and polymers are used as precipitants.
1.1 Salts
A rather limited set of salts (which can be found in the Alphabetical List below) has been used to produce protein and nucleic acid crystals. For most crystallizations it is essential to find the optimal salt concentration, which may be anywhere between 15 and 85% saturation. This value must be defined to a precision of 1-2%. Ammonium sulfate is the most widely used precipitant of the salt type. Citrate salts, due to their chelating properties, may be especially useful when the presence of divalent cations interferes with crystallization. Cetyltrimethylammonium salts are exceptional, since they increase the solubility of macromolecules in the crystallization solution with increasing concentration.
1.2 Organic Solvents
Organic solvents used for the crystallization of biopolymers can be found in the Alphabetical List. The optimal concentration of the organic solvent for the crystallization of a given biopolymer has to be ascertained with a precision of 1-2%, from a large concentration range, as in the case with salt-type precipitants. In contrast to salt type precipitants, organic solvents can easily denature biopolymers. 2-methyl-2,4-pentanediol for example has been found to be a quite mild and efficient precipitant for otherwise sensitive macromolecules. 2-Methyl-2, 4-pentanediol, also known as MPD or hexylene glycol, is the most widely used precipitant of the organic solvent type.
1.3 Polymers
The most widely used polymers for crystallization are the polyethylene glycols. Fluka has recently introduced PEG with the molecular weights 1000, 3000, 6000 and 8000 in the unique BioChemika Ultra quality.
2. Auxiliary Substances
Additional substances for crystallization may be of importance in more special cases. The presence of small polyamines, such as spermine, cadaverine, spermidine or putrescine, in the crystallization solution seems to be mandatory for the growth of high quality crystals of transfer RNA. These polyamines probably act as specific counterions for the negatively charged phosphate groups. X-ray crystallographic studies of polymorphic forms of yeast phenylalanine transfer RNA [15] have clearly shown the potential of this method [16].
With the exception of the concentration of the precipitant, the most important variable in the search for crystallization conditions is the pH value. A large variety of buffer substances (cf. section on "Biological Buffers") are available from Fluka.
Since crystal growth generally requires time to reach completion, exposure to oxygen is likely to occur. It therefore may be wise to include a mild antioxidant (cf. section on "Antioxidants") such as cysteine, -mercaptoethanol, glutathione or dithiothreitol in the crystallization solution.
Metal ions (listed under "Salts") may improve the crystallization of proteins irrespective of whether the ion is the cofactor of the apoprotein or not. Chelating agents, such as EDTA, have to be added to the crystallization solution if metal cations prevent crystal formation. Furthermore, a variety of small molecules and ions have been found to affect the crystallization process [1].
To meet highest demands for quality Fluka offers a wide range of BioChemika Ultra standard products.
References
A. McPherson, Preparation and Analysis of Protein Crystals, John Wiley and Sons, New York (1982).
Crystallization and Treatment of Crystals, Methods Enzymol. 114, Sect II, 49 (1985).
Theory of protein solubility: T. Arakawa, S.N.Timasheff, Methods Enzymol, 114, 49 (1985).
Nucleation and growth of protein crystals: general principles and assays: G. Feher, Z.Kam, Methods Enzymol. 114, 77 (1985).
Crystallization of macromolecules: general principles: A. McPherson, Methods Enzymol. 114, 112 (1985).
Crystallization of ps: R. Giegi, in: Crystallography in Molecular Biology (D. Moras et al., eds.), p. 15, Plenum Press, New York (1987).
Protein crystallization.rotein and nucleic acids: a survey of methods and importance of the purity of the macromolecule The growth of large-scale single crystals: G. L. Gilliland, D. R. Davies, Methods Enzymol. 104, 370 (1984).
Determination of a transfer RNA structure by crystallographic methods: S.-H.Kim, G.J.Quigley, Methods Enzymol.59, 3 (1979).
Experimental neutron protein crystallography: B. P. Schoenborn, Methods Enzymol. 114, 510 (1985).
The application of neutron crystallography to the study of dynamic and hydration properties of proteins: A. A. Kossiakoff, Ann. Rev. Biochem. 54 1195 (1985).
New directions in protein crystal growth: L.J. Deluca, C. E. Bugg, Trends N Biotechnol.5, 188 (1987).
The future of protein crystal growth: C. E. Bugg, J. Cryst. Growth 76, 535 (1986).
R. Henderson, D. N. T. Unwin, Nature 257 28 (1975).
R.Arad et al.,Anal.Biochem.167, 112 (1987).
S.H.Kim et al.,J.Mol.Biol.75,421 (1973).
J.E.Ladner et al., J.Mol.Biol.72, 99 (1972).
List of Products
A-C D-N P R-S T-Z
Catalog No. Name see
A-C
Acetic acid magnesium salt Magnesium acetate
Acetic acid sodium salt Sodium acetate
2-Amino-2-(hydroxymethyl)-1,3-propanediol Trizma® base
N-(3-Aminopropyl)-1,4-diaminobutane Spermidine
Ammonium dihydrogen phosphate Ammonium phosphate monobasic
Ammonium hydrogen sulfate Ammonium bisulfate
Ammonium sodium hydrogen phosphate Ammonium sodium phosphate dibasic tetrahydrate
Ammonium sulfate monobasic Ammonium bisulfate
09688 Ammonium acetate for molecular biology
09689 Ammonium acetate
09847 Ammonium bisulfate
09711 Ammonium chloride
09718 Ammonium chloride for molecular biology
88163 Ammonium chloride solution for molecular biology
09833 Ammonium citrate dibasic
09889 Ammonium nitrate
09839 Ammonium phosphate dibasic
70705 Ammonium phosphate dibasic solution
09709 Ammonium phosphate monobasic
Mono-ammonium phosphate Ammonium phosphate monobasic
prim-Ammonium phosphate Ammonium phosphate monobasic
75568 Ammonium phosphate monobasic solution
71284 Ammonium sodium phosphate dibasic tetrahydrate
09978 Ammonium sulfate
83267 Ammonium sulfate solution for molecular biology
09985 Ammonium tartrate dibasic
70631 Ammonium tartrate dibasic solution
Benzoic acid sodium salt Sodium benzoate
83263 BICINE buffer Solution for molecular biology
N,N'-Bis(3-aminopropyl)-1,4-diaminobutane Spermine
N,N-Bis(2-hydroxyethyl)glycine BICINE
Buffer solution 1 M pH 3.0, TEAP Triethylammonium phosphate solution
Buffer solution 1 M pH 7.0 (volatile) Triethylammonium acetate buffer
Butanedioic acid disodium salt Sodium succinate dibasic
21056 Calcium acetate hydrate
21097 Calcium chloride dihydrate for molecular biology
21098 Calcium chloride dihydrate
21108 Calcium chloride hexahydrate
21115 Calcium chloride solution for molecular biology
Carbamide Urea
Carbonyldiamide Urea
Cetrimide Hexadecyltrimethylammonium bromide
Cetrimonium bromide Hexadecyltrimethylammonium bromide
Cetyltrimethylammonium bromide Hexadecyltrimethylammonium bromide
Chile salpeter Sodium nitrate
Citric acid Ammonium citrate dibasic
Citric acid monosodium salt Sodium citrate monobasic
Citric acid trisodium salt 'Sodium citrate tribasic
CTAB Hexadecyltrimethylammonium bromide
Catalog No. Name see
D-N
49139 Dextrose
1,8-Diamino-4-azaoctane Spermidine
Diammonium hydrogen citrate Ammonium citrate dibasic
Diammonium tartrate Ammonium tartrate dibasic
Diammonium hydrogen phosphate Ammonium phosphate dibasic
di-Ammonium hydrogen phosphate (sec) Ammonium phosphate dibasic
D-2,3-Dihydroxybutanedioic acid monopotassium salt Potassium D-tartrate monobasic
Dipotassium hydrogen phosphate Potassium phosphate dibasic
Dipotassium phosphate Potassium phosphate dibasic
Disodium hydrogen phosphate Sodium phosphate dibasic
Disodium phosphate Sodium phosphate dibasic
Disodium tartrate dihydrate Sodium tartrate dibasic
Di(tris[hydroxymethyl]aminomethane) carbonate Trizma® carbonate
Dodecyl lithium sulfate Lithium dodecyl sulfate
Dodecyl sulfate lithium salt Lithium dodecyl sulfate
Epsom salts Magnesium sulfate heptahydrate
Ethanediol Ethylene glycol
03747 Ethylene glycol
Formic acid potassium salt Potassium formate
Formic acid sodium salt Sodium formate
Gerontine Spermine
Glauber's salt Sodium sulfate
49139 D-(+)-Glucose
Glycol Ethylene glycol
52365 Hexadecyltrimethylammonium bromide for molecular biology
52369 Hexadecyltrimethylammonium bromide
88571 1,6-Hexanediol solution
Hexylene glycol (±)-2-Methyl-2,4-pentanediol
Isobutanol 2-Methyl-1-propanol for molecular biology
Isobutyl alcohol 2-Methyl-1-propanol for molecular biology
Isopropanol 2-Propanol
Isopropyl alcohol 2-Propanol
Lithium lauryl sulfate Lithium dodecyl sulfate
62393 Lithium acetate dihydrate
73216 Lithium acetate solution
62476 Lithium chloride for molecular biology
62477 Lithium chloride
62479 Lithium chloride solution for molecular biology
83268 Lithium chloride solution for molecular biology
62554 Lithium dodecyl sulfate
62612 Lithium sulfate monohydrate
82348 Lithium sulfate solution
63052 Magnesium acetate solution for molecular biology
63049 Magnesium acetate tetrahydrate
63064 Magnesium chloride hexahydrate
63068 Magnesium chloride hexahydrate for molecular biology
63036 Magnesium chloride solution for molecular biology
63069 Magnesium chloride solution for molecular biology
68475 Magnesium chloride solution for molecular biology
63084 Magnesium nitrate hexahydrate
83270 Magnesium nitrate solution for molecular biology
63138 Magnesium sulfate heptahydrate
63137 Magnesium sulfate hydrate
63133 Magnesium sulfate solution for molecular biology
83266 Magnesium sulfate solution for molecular biology
63535 Manganese(II) chloride tetrahydrate for molecular biology
Methoxypolyethylene glycol Polyethylene glycol monomethyl ether
mono-Methyl polyethylene glycol Polyethylene glycol monomethyl ether
68338 (±)-2-Methyl-2,4-pentanediol
58448 2-Methyl-1-propanol for molecular biology
Monosodium phosphate Sodium phosphate monobasic
MPD (±)-2-Methyl-2,4-pentanediol
Musculamine Spermine
Neuridine Spermine
2,2',2''-Nitrilotriethanol Triethanolamine
Catalog No. Name see
P
Palmityltrimethylammonium bromide Hexadecyltrimethylammonium bromide
PEG Polyethylene glycol
81188 Polyethylene glycol
81189 Polyethylene glycol for molecular biology
81227 Polyethylene glycol
81253 Polyethylene glycol for molecular biology
81255 Polyethylene glycol
81268 Polyethylene glycol for molecular biology
84797 Polyethylene glycol
86101 Polyethylene glycol
87333 Polyethylene glycol
88276 Polyethylene glycol
88440 Polyethylene glycol
89510 Polyethylene glycol
90878 Polyethylene glycol
91893 Polyethylene glycol
92897 Polyethylene glycol
94646 Polyethylene glycol
95904 Polyethylene glycol
73034 Polyethylene glycol solution for molecular biology
76293 Polyethylene glycol solution for molecular biology
81304 Polyethylene glycol solution for molecular biology
83271 Polyethylene glycol solution for molecular biology
83272 Polyethylene glycol solution for molecular biology
84184 Polyethylene glycol solution for molecular biology
87006 Polyethylene glycol solution for molecular biology
87006 Polyethylene glycol solution for molecular biology
89782 Polyethylene glycol solution for molecular biology
81269 Polyethylene glycol 3'000 monodispers solution
71578 Polyethylene glycol monomethyl ether
83918 Polyethylene glycol monomethyl ether solution for molecular biology
90364 Polyethylene glycol monomethyl ether solution for molecular biology
Potassium bichromate Potassium dichromate
Potassium hydrogen D-tartrate Potassium D-tartrate monobasic
sec.-Potassium phosphate Potassium phosphate dibasic
tert-Potassium phosphate Potassium phosphate tribasic
Potassium rhodanide Potassium thiocyanate
60033 Potassium acetate
60035 Potassium acetate for molecular biology
60041 Potassium acetate for luminescence
60038 Potassium acetate solution for molecular biology
60039 Potassium acetate solution for molecular biology
95843 Potassium acetate solution for molecular biology
60128 Potassium chloride for molecular biology
60129 Potassium chloride
60135 Potassium chloride solution
60142 Potassium chloride solution for molecular biology
87526 Potassium chloride solution
60139 Potassium chromate
89306 Potassium citrate tribasic solution
60188 Potassium dichromate
60246 Potassium formate
78716 Potassium formate solution
60414 Potassium nitrate
60352 Potassium phosphate dibasic for luminescence
60353 Potassium phosphate dibasic for molecular biology
60354 Potassium phosphate dibasic
79713 Potassium phosphate dibasic solution
60494 Potassium phosphate tribasic monohydrate
81028 Potassium sodium tartrate solution
60413 Potassium sodium tartrate tetrahydrate
60366 Potassium D-tartrate monobasic
60517 Potassium thiocyanate
73059 Potassium thiocyanate solution
59304 2-Propanol for molecular biology
sec-Propyl alcohol 2-Propanol
Catalog No. Name see
R-S
Rochelle salt Potassium sodium tartrate
Salmiac Ammonium chloride
Seignette salt Potassium sodium tartrate
Sodium ammonium hydrogen phosphate Ammonium sodium phosphate dibasic tetrahydrate
sec-Sodium ammonium phosphate Ammonium sodium phosphate dibasic tetrahydrate
Sodium dihydrogen citrate Sodium citrate monobasic
Sodium dihydrogen phosphate monohydrate Sodium phosphate monobasic
Sodium hydrogen tartrate Sodium bitartrate
sec-Sodium phosphate Sodium phosphate dibasic
Sodium rhodanide solution Sodium thiocyanate solution
Sodium tartrate dihydrate Sodium tartrate dibasic
71179 Sodium acetate
71183 Sodium acetate for molecular biology
71184 Sodium acetate for luminescence
71196 Sodium acetate solution for molecular biology
71188 Sodium acetate trihydrate
71289 Sodium azide
71295 Sodium benzoate
71679 Sodium bitartrate monohydrate
71376 Sodium chloride for molecular biology
71378 Sodium chloride
71497 Sodium citrate monobasic
71401 Sodium citrate tribasic dihydrate for luminescence
71402 Sodium citrate tribasic dihydrate for molecular biology
71404 Sodium citrate tribasic dihydrate
83273 Sodium citrate tribasic solution for molecular biology
71519 Sodium fluoride
71539 Sodium formate
74293 Sodium formate solution
71755 Sodium nitrate
71636 Sodium phosphate dibasic for molecular biology
71637 Sodium phosphate dibasic dihydrate for luminescence
71649 Sodium phosphate dibasic dodecahydrate
94046 Sodium phosphate dibasic solution
71507 Sodium phosphate monobasic monohydrate for molecular biology
74092 Sodium phosphate monobasic solution
71908 Sodium phosphate tribasic dodecahydrate
14158 Sodium succinate dibasic hexahydrate
71959 Sodium sulfate
71969 Sodium sulfate decahydrate
71994 Sodium tartrate dibasic dihydrate
79299 Sodium tartrate dibasic Solution
72028 Sodium tetrathionate dihydrate
80518 Sodium thiocyanate solution
85558 Spermidine for molecular biology
85559 Spermidine
85578 Spermidine trihydrochloride
85588 Spermine dihydrate
85605 Spermine tetrahydrochloride for molecular biology
85607 Spermine tetrahydrochloride
Succinic acid disodium salt Sodium succinate dibasic
Catalog No. Name see
T-Z
L-(+)-Tartaric acid diammonium salt Ammonium tartrate dibasic
L-(+)-Tartaric acid disodium salt Sodium tartrate dibasic
D-(-)-Tartaric acid monopotassium salt Potassium D-tartrate monobasic
L-(+)-Tartaric acid monosodium salt Sodium bitartrate
L(+)-Tartaric acid potassium sodium salt Potassium sodium tartrate
TEA chloride Tetraethylammonium chloride
86614 Tetraethylammonium chloride for molecular biology
87718 Tetramethylammonium chloride for molecular biology
THAM Trizma® base
90278 Triethanolamine
90357 Triethylammonium acetate buffer
90361 Triethylammonium phosphate solution
95126 Triethylene glycol
96924 2,2,2-Trifluoroethanol for molecular biology
Trifluoroethyl alcohol 2,2,2-Trifluoroethanol
Triglycol Triethylene glycol
Tripotassium phosphate Potassium phosphate tribasic
Tris base Trizma® base
TRIS carbonate Trizma® carbonate
TRIS HCl Trizma® hydrochloride
TRIS hydrochloride Trizma® hydrochloride
Tris(2-hydroxyethyl)amine Triethanolamine
Tris(hydroxymethyl)aminomethane Trizma® base
Tris(hydroxymethyl)aminomethane acetate salt Trizma® acetate
Tris(hydroxymethyl)aminomethane carbonate Trizma® carbonate
Tris(hydroxymethyl)aminomethane hydrochloride Trizma® hydrochloride
Tris acetate Trizma® acetate
Trisodium citrate 'Sodium citrate tribasic
Trisodium phosphate dodecahydrate Sodium phosphate tribasic
93337 Trizma® acetate
08656 Trizma® base
93286 Trizma® base for luminescence
93349 Trizma® base
93362 Trizma® base
93362 Trizma® base for molecular biology
93327 Trizma® carbonate
93287 Trizma® hydrochloride for luminescence
93358 Trizma® hydrochloride
93363 Trizma® hydrochloride for molecular biology
41573 Trizma® hydrochloride buffer solution for molecular biology
93313 Trizma® hydrochloride buffer solution for molecular biology
93314 Trizma® hydrochloride buffer solution for molecular biology
93316 Trizma® hydrochloride buffer solution for molecular biology
Trometamol Trizma® base
TSP Sodium phosphate tribasic
02493 Urea for DNA sequencing
51456 Urea for molecular biology
51458 Urea
51457 Urea solution
70331 Zinc acetate solution for molecular biology
96468 Zinc chloride for molecular biology
83265 Zinc sulfate solution for molecular biology
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2007-01-18 11:08:09
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answer #4
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answered by Anonymous
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0⤊
0⤋