A seed can provide a template on which additional macromolecules can assemble and under the proper conditions, grow to form a large single crystal. Using seeding can avoid problems associated with growing crystals from spontaneous nucleation. Seeds can grow into larger crystals in the metastable region of the solubility curve, which is a region of lower, relative supersaturation. One can also streak seed from phase separation or amorphous material as a diagnostic to confirm whether the material is crystalline.

The Seeding Tool is a 1 cm natural fiber attached to a stainless steel pin and plastic handle. The Seeding Tool is supplied with a cover to protect the fiber and when the cover is placed on the back side of the Seeding Tool, it makes an excellent handle.

Seeding Tool

1. Seeds to crystals. Terese Bergfors. Journal of Structrual Biology 142 (2003) 66-76.

2. Applications of the streak seeding technique in protein crystallization. Stura and Wilson. Journal of Crystal Growth, 110 (1991) 270-282. 110 (1991) 270-282.

3. Applications of the streak seeding technique in protein crystallization. Stura and Wilson. Journal of CrystaL Growth, 110 (1991) 270-282.

4. Crystallization of pig mitochondrial aspartate aminotransferase by seeding with crystals of the chicken mitochondrial isoenzyme. Eichele G, Ford GC, Jansonius JN. J Mol Biol. 1979 Dec 5;135(2):513-6. PubMed PMID: 537086.

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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Cryschem S microplate approximate size: 128 mm x 86 mm x 14 mm
Approximate square reservoir size: 15 mm wide x 9 mm deep
Typical reservoir volume: 500 µl
Well capacity: 1.1 ml
Maximum drop volume on post: 30 µl

Recommended seal:
HR3-609 Crystal Clear Sealing Film (100 pack)
HR4-521 ClearSeal Film (100 pack)
HR4-506 Crystal Clear Sealing Tape (3 inch x 55 yard roll, without cutter)
HR4-508 Crystal Clear Sealing Tape (0.75 inch x 650 inch, with cutter) seals a single row at a time

Cryschem S Plate (square reagent reservoir)

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: Formic acid magnesium salt
C₂H₂O₄Mg • 2H₂O
M_r 150.38
CAS Number [6150-82-9]
EC Number 209-173-9
MDL Number MFCD00150512
PubChem Substance ID 24845074
Beilstein Registry Number 3725251
Purity 98.5%

Measured pH Range: 7.6 – 7.8 at 25°C
Measured Conductivity Range: 45.6 – 53.3 mS/cm at 25°C
Measured Refractive Index Range: 1.35203 – 1.35266 at 20°C

1.0 M Magnesium formate dihydrate

1. Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme from Thermus thermophilus. M. N. Vassylyeva, J. Lee, S. Sekine, O. Laptenko, S. Kuramitsu, T. Shibata, Y. Inoue, S. Borukhov, D. G. Vassylyev and S. Yokoyama. Acta D, Volume 58, Part 9 (September 2002).

2. Expression, purification, crystallization and preliminary X-ray crystallographic studies of a novel acetylcitrulline deacetylase from Xanthomonas campestris. D. Shi, X. Yu, L. Roth, H. Morizono, Y. Hathout, N. M. Allewell and M. Tuchman. Acta Cryst. (2005). F61, 676-679.

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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Why Sandwich Boxes? They allow one to use very, very large drops. They are optically superior to plastic plates and glass slides, and offer different equilibration kinetics than other crystallization plates. Each of the Sandwich Box components can be washed and reused so there is little waste with the Sandwich Box Setup. These plates can be used during screening and optimization, but are best suited for final optimization and production of crystals. Since the glass plates can be removed from the boxes, crystal mounting is convenient. The siliconized 9 well depression plates are also useful for heavy atom soaks, cryo solution dilution and transfers, and seeding experiments where serial dilutions are involved. Sandwich Box Setups are available as a complete set or as individual components so one can customize the system to meet their needs. Square cover slides can be used to seal individual reservoirs but are not typically used in a crystallization setup. The Sandwich Box Setup consists of a square plastic box (4 5/16” x 4 5/16” x 1 1/8”), a polystyrene plate support, and a siliconized, glass plate (4” L x 3 3/8” W (100 mm x 85 mm)) with nine concave depressions (7/8” O.D. x 1/4” D (22 mm x 7 mm)).

Drop sizes up to 800 microliters are possible with the Sandwich Box Setup.

Sandwich Box Setup

Siliconized 9 Well Glass Plate

Sandwich Box with cover

1. In situ X-ray crystallography. A. McPherson. J. Appl. Cryst. (2000). 33, 397-400.

2. Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum. Kovalevsky, A. Y., Hanson, B. L., Seaver, S., Fisher, S. Z., Mustyakimov, M. & Langan, P. (2011). Acta Cryst. F67, 283-286.

3. Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments. Acta Crystallographica Section D Structural Biology. 75. 10.1107/S2059798319012695.   Andersson, Rebecka & Safari, Cecilia & Båth, Petra & Bosman, Robert & Shilova, Anastasya & Dahl, Peter & Ghosh, Swagatha & Dunge, Andreas & Kjeldsen-Jensen, Rasmus & Nan, Jie & Shoeman, Robert & Kloos, Marco & Doak, R. & Mueller, Uwe & Neutze, Richard & Brändén, Gisela. (2019). 

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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Cryschem plate approximate size: 15.0 cm x 10.6 cm x 2.2 cm
Approximate well size: 1.6 cm x 1.5 cm
Typical fill volume: 500 to 1,000 µl
Well capacity: 1.5 ml
Maximum drop volume on post: 40 µl

Recommended seal:
HR3-511 Crystal Clear Sealing Tape (1.88 inch x 43.7 yard roll, with cutter)
HR4-511 Crystal Clear Sealing Tape (1.88 inch x 60 yard roll, without cutter)

Cryschem Plate

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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Overall length: ~ 43 mm
Diameter of handle: ~ 3 mm
Diameter of hemispherical end: ~ 1 mm

Five Crystal Crushers per pack.

Crystal Crusher

1. Microseed matrix screening for optimization in protein crystallization: what have we learned? D’Arcy A, Bergfors T, Cowan-Jacob SW, Marsh M. Acta Crystallogr F Struct Biol Commun. 2014 Sep;70 (Pt 9):1117-26. doi: 10.1107/S2053230X14015507. Epub 2014 Aug 29.

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: Magnesium nitrate
Mg(NO₃)₂ • 6H₂O
MgN₂O₆ • 6H₂O
M_r 256.41
CAS [13446-18-9]
EC Number 233-826-7
Merck 14,5674
RTECS Number OM3756000
UN Number 1474 5.1/PG
MDL Number MFCD00149779
PubChem Substance ID 24882354
Purity ≥ 99.0%

Measured pH Range: 2.7 – 4.2 at 25°C
Measured Conductivity Range: 112.4 – 137.0 mS/cm at 25°C
Measured Refractive Index Range: 1.39348 – 1.39373 at 20°C

Al ≤0.0005%
As ≤0.00001%
Ba ≤0.001%
Bi  ≤0.001%
Ca ≤0.5%
Cd ≤0.0005%
Cl ≤0.005%
Co ≤0.0005%
Cr ≤0.0005%
Cu ≤0.0005%
Fe ≤0.0005%
K  ≤0.01%
Li  ≤0.0005%
Mn ≤0.0005%
Mo ≤0.0005%
Na ≤0.01%
Ni  ≤0.0005%
Pb  ≤0.0005%
SO₄ ≤0.005%
Sr  ≤0.001%
Zn ≤0.0005%

3.0 M Magnesium nitrate hexahydrate

1. Crystallization and preliminary X-ray diffraction studies on the catalytic domain of the chick retinal neurite-inhibitory factor CRYP-2. T. S. Girish and B. Gopal. Acta Cryst. (2005). F61, 381-383.

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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Tungsten carbide scribe tips are not threaded and are held in place with a threaded tip chuck. To remove tip, turn the tip chuck counterclockwise one turn (without completely removing the chuck) while holding the aluminum handle stationary, and pull the tip from the chuck and handle. To install a new tip, slide the new tip into the chuck and handle and tighten the tip chuck clockwise to secure the new tip into the handle. Loosen tip chuck, remove tip, reserve and install with the tip inverted to protect user and the tip when not in use.

Tungsten Carbide Scribe is supplied with one tip installed. Replacement tips sold separately. Tungsten Carbide Scribe Tip is a set of 3 replacement tips designed for the Tungsten Carbide Scribe HR4-702. Tungsten carbide Tip in steel shank to strengthen and protect carbide from damage. Scribe Tip Diameter x Length: 3 mm X 32 mm.

See the JOVE video for more details about using the Tungsten Carbide glass cutter to open LCP Sandwich Set experiments:

Tungsten Carbide Scribe

Tungsten Carbide Scribe Tip

1. Li, D., Boland, C., Walsh, K., Caffrey, M. Use of a Robot for High-throughput Crystallization of Membrane Proteins in Lipidic Mesophases. J. Vis. Exp. (67), e4000, DOI: 10.3791/4000 (2012).

2. Cherezov, V., and M. Caffrey. (2003) Nano-volume plates with excellent optical properties for fast, inexpensive crystallization screening of membrane proteins. J. Appl. Cryst. 36: 1372-1377.

3. Cherezov, V., Peddi, A., Muthusubramaniam, L., Zheng, Y.F., and M. Caffrey. (2004) A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases. Acta Crystallogr. D Biol. Crystallogr. 60: 1795-1807.

4. Caffrey, M., Li, D., & Dukkipati, A. Membrane protein structure determination using crystallography and lipidic mesophases – recent advances and successes. Biochemistry. DOI: 10.1021/bj300010w, 2012.

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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15.0 cm x 10.8 cm plate footprint is convenient for manual pipetting and well access while at the same time compatible with some automated liquid handling systems.
Approximate dimensions: 15.0 cm x 10.6 cm x 2.2 cm.
Approximate well size: 1.7 cm x 1.6 cm.
Typical well volume: 500 to 1,000 µl.
Well capacity: 3.5 ml.

VDX™ Plate without sealant

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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Seeding allows one to grow crystals in the metastable zone. Crystallization in this zone provides control, reproducibility and an improved likelihood of a successful crystallization experiment. Also, crystals can grow from seeds but cannot spontaneously nucleate. By placing a seed or solution of seeds in a drop which is saturated to the metastable zone, one can use the seeds to grow larger single crystals. By controlling the number of seeds introduced into the drop, one can control the number of crystals grown. It is not practically possible to measure and know the number of seeds introduced to a drop, but by performing serial dilutions from a concentrated seed stock, one can control the number of crystals grown in the drop.

Using the Seed Bead kits, one can create crystal seed stock for subsequent seeding experiments. Crystals are placed in the microcentrifuge tube with the Seed Bead(s) and either vortexed or sonicated to generate a seed stock. Then by performing serial dilutions, one can control the number and size of crystals in the experiment.

The Seed Bead kit is useful for the preparation of seed stocks for automated and semi-automated microseeding (D’Arcy 2007, Harlos 2008).

Each Seed Bead Kit (HR2-320) contains 24 special microcentrifuge tubes, each tube containing a single 3mm PTFE Seed Bead.

Each Seed Bead Steel Kit (HR4-780) contains 24 special microcentrifuge tubes, each tube containing a six 1.6 mm Stainless Steel Seed Beads.

Each Seed Bead Ceramic Kit (HR4-781) contains 24 special microcentrifuge tubes, each tube containing a ten 1.0 mm Zirconium Silicate Ceramic Seed Beads.

Each Seed Bead Glass Kit (HR4-782) contains 24 special microcentrifuge tubes, each tube containing a ten 1.0 mm Glass Seed Beads.

Seed Bead Kit

Seed Bead Steel Kit

Seed Bead Ceramic Kit

Seed Bead Glass Kit

1. Stura, E.A., Wilson, I.A., Methods: A Companion to Methods in Enzymology (1990) 1, 38-49.

2. Stura, E.A., Wilson, I.A., “Seeding Techniques” in Crystallization of Nucleic Acids and Proteins: A Practical Approach. Oxford University Press (1992) 99-126.

3. A method to produce microseed stock for use in the crystallization of biological macromolecules Luft, J.R., DeTitta, G.T. Acta Cryst. (1999). D55, 988-993.

4. J.R. Luft and G.T. DeTitta, Methods in Enzymology (1997) 276, 110-131.

5. Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement. Watanabe et al. Acta Cryst. (2006). D62, 784-792.

6. Crystallization and preliminary crystallographic analysis of p40phox, a regulatory subunit of NADPH oxidase. K. Honbou, S. Yuzawa, N. N. Suzuki, Y. Fujioka, H. Sumimoto and F. Inagaki. Acta Cryst. (2006). F62, 1021-1023 (Used seed bead to optimize)

7. Purification, crystallization and preliminary X-ray diffraction study of human ribosomal protein L10 core domain. Yuji Kobayashi et al. Acta Cryst. (2007). F63, 950-952

8. An automated microseed matrix-screening method. Allan D′Arcy, Frederic Villard and May Marsh. Acta Cryst. (2007). D63, 550-554

9. The role of bias in crystallization conditions in automated microseeding. Edwin Pozharski et al. Acta Cryst. (2008). D64, 1222-1227.

10. Transmission electron microscopy for the evaluation and optimization of crystal growth. Hilary P. Stevenson & Guillermo Calero et al. Acta Cryst. (2016) D72, 603-615.

11. Microseed matrix screening for optimization in protein crystallization: what have we learned? D’Arcy A, Bergfors T, Cowan-Jacob SW, Marsh M. Acta Crystallogr F Struct Biol Commun. 2014 Sep;70 (Pt 9):1117-26. doi: 10.1107/S2053230X14015507. Epub 2014 Aug 29.

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: Epsom salts
MgSO₄ • 7H₂O
M_r 246.47
CAS Number 10034-99-8
EC Number 231-298-2
Merck 14,5691
RTECS OM4508000
MDL Number MFCD00149785
PubChem Substance ID 24882416
Purity ≥ 99.5%

Measured pH Range: 5.0 – 7.0 at 25°C
Measured Conductivity Range: 51.8 – 58.1 mS/cm at 25°C
Measured Refractive Index Range: 1.37383 – 1.37468 at 20°C

Al  ≤0.0005%
As ≤0.00001%
Ba ≤0.0005%
Bi  ≤0.0005%
Ca ≤0.001%
Cd ≤0.0005%
Cl ≤0.0005%
Co ≤0.0005%
Cr ≤0.0005%
Cu ≤0.0005%
Fe ≤0.0001%
K  ≤0.001%
Li  ≤0.0005%
Mn ≤0.0005%
Mo ≤0.0005%
N  ≤0.002%
Na ≤0.001%
Ni ≤0.0005%
Pb ≤0.0005%
Sr ≤0.0005%
Zn ≤0.0005%

2.0 M Magnesium sulfate heptahydrate

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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Detergent Screen 01 (A01) 0.5 mL

Detergent Screen 02 (A02) 0.5 mL

Detergent Screen 03 (A03) 0.5 mL

Detergent Screen 04 (A04) 0.5 mL

Detergent Screen 05 (A05) 0.5 mL

Detergent Screen 06 (A06) 0.5 mL

Detergent Screen 07 (A07) 0.5 mL

Detergent Screen 08 (A08) 0.5 mL

Detergent Screen 09 (A09) 0.5 mL

Detergent Screen 10 (A10) 0.5 mL

Detergent Screen 11 (A11) 0.5 mL

Detergent Screen 12 (A12) 0.5 mL

Detergent Screen 13 (B01) 0.5 mL

Detergent Screen 14 (B02) 0.5 mL

Detergent Screen 15 (B03) 0.5 mL

Detergent Screen 16 (B04) 0.5 mL

Detergent Screen 17 (B05) 0.5 mL

Detergent Screen 18 (B06) 0.5 mL

Detergent Screen 19 (B07) 0.5 mL

Detergent Screen 20 (B08) 0.5 mL

Detergent Screen 21 (B09) 0.5 mL

Detergent Screen 22 (B10) 0.5 mL

Detergent Screen 23 (B11) 0.5 mL

Detergent Screen 24 (B12) 0.5 mL

Detergent Screen 25 (C01) 0.5 mL

Detergent Screen 26 (C02) 0.5 mL

Detergent Screen 27 (C03) 0.5 mL

Detergent Screen 28 (C04) 0.5 mL

Detergent Screen 29 (C05) 0.5 mL

Detergent Screen 30 (C06) 0.5 mL

Detergent Screen 31 (C07) 0.5 mL

Detergent Screen 32 (C08) 0.5 mL

Detergent Screen 33 (C09) 0.5 mL

Detergent Screen 34 (C10) 0.5 mL

Detergent Screen 35 (C11) 0.5 mL

Detergent Screen 36 (C12) 0.5 mL

Detergent Screen 37 (D01) 0.5 mL

Detergent Screen 38 (D02) 0.5 mL

Detergent Screen 39 (D03) 0.5 mL

Detergent Screen 40 (D04) 0.5 mL

Detergent Screen 41 (D05) 0.5 mL

Detergent Screen 42 (D06) 0.5 mL

Detergent Screen 43 (D07) 0.5 mL

Detergent Screen 44 (D08) 0.5 mL

Detergent Screen 45 (D09) 0.5 mL

Detergent Screen 46 (D10) 0.5 mL

Detergent Screen 47 (D11) 0.5 mL

Detergent Screen 48 (D12) 0.5 mL

Detergent Screen 49 (E01) 0.5 mL

Detergent Screen 50 (E02) 0.5 mL

Detergent Screen 51 (E03) 0.5 mL

Detergent Screen 52 (E04) 0.5 mL

Detergent Screen 53 (E05) 0.5 mL

Detergent Screen 54 (E06) 0.5 mL

Detergent Screen 55 (E07) 0.5 mL

Detergent Screen 56 (E08) 0.5 mL

Detergent Screen 57 (E09) 0.5 mL

Detergent Screen 58 (E10) 0.5 mL

Detergent Screen 59 (E11) 0.5 mL

Detergent Screen 60 (E12) 0.5 mL

Detergent Screen 61 (F01) 0.5 mL

Detergent Screen 62 (F02) 0.5 mL

Detergent Screen 63 (F03) 0.5 mL

Detergent Screen 64 (F04) 0.5 mL

Detergent Screen 65 (F05) 0.5 mL

Detergent Screen 66 (F06) 0.5 mL

Detergent Screen 67 (F07) 0.5 mL

Detergent Screen 68 (F08) 0.5 mL

Detergent Screen 69 (F09) 0.5 mL

Detergent Screen 70 (F10) 0.5 mL

Detergent Screen 71 (F11) 0.5 mL

Detergent Screen 72 (F12) 0.5 mL

Detergent Screen 73 (G01) 0.5 mL

Detergent Screen 74 (G02) 0.5 mL

Detergent Screen 75 (G03) 0.5 mL

Detergent Screen 76 (G04) 0.5 mL

Detergent Screen 77 (G05) 0.5 mL

Detergent Screen 78 (G06) 0.5 mL

Detergent Screen 79 (G07) 0.5 mL

Detergent Screen 80 (G08) 0.5 mL

Detergent Screen 81 (G09) 0.5 mL

Detergent Screen 82 (G10) 0.5 mL

Detergent Screen 83 (G11) 0.5 mL

Detergent Screen 84 (G12) 0.5 mL

Detergent Screen 85 (H01) 0.5 mL

Detergent Screen 86 (H02) 0.5 mL

Detergent Screen 87 (H03) 0.5 mL

Detergent Screen 88 (H04) 0.5 mL

Detergent Screen 89 (H05) 0.5 mL

Detergent Screen 90 (H06) 0.5 mL

Detergent Screen 91 (H07) 0.5 mL

Detergent Screen 92 (H08) 0.5 mL

Detergent Screen 93 (H09) 0.5 mL

Detergent Screen 94 (H10) 0.5 mL

Detergent Screen 95 (H11) 0.5 mL

Detergent Screen 96 (H12) 0.5 mL

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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15.0 cm x 10.8 cm plate footprint is convenient for manual pipetting and well access while at the same time compatible with some automated liquid handling systems.
Approximate dimensions: 15.0 cm x 10.6 cm x 2.2 cm.
Approximate well size: 1.7 cm x 1.6 cm.
Typical well volume: 500 to 1,000 µl.
Well capacity: 3.5 ml.

VDX™ Plate with sealant

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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Glass Fiber

Glass Fiber

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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