Hampton蛋白结晶试剂盒LCP Sandwich Set

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LCP Sandwich Set

Applications

  • Crystallization screening of membrane proteins in lipidic mesophase as well as bicelle method and batch method

Features

  • Small volume LCP, bicelle and microbatch crystallization
  • High quality glass optics
  • Excellent drop optics since mesophase bolus is physically sandwiched between two optically clear surfaces eliminating the mesophase / aqueous medium interface and the corresponding roughness
  • Glass plate allows for visualization of microcrystals using birefringence-free examination between crossed polarizers
  • Superhydrophobic glass surfaces
  • Optimized for bright field, UV and fluorescent microscopy
  • Excellent stability, resistant to evaporation

Description

The LCP Sandwich Set consists of a base glass slide and an optimized cover slip. LCP Sandwich Set developed jointly with the renowned Scripps Research Institute in La Jolla, California, USA and is manufactured by Paul Marienfeld (0890003).

The LCP Glass Sandwich Set is a specially designed plate for either automated or manual setting of 96 Lipidic Cubic Phase matrix screening experiments. The plate can also be used for the bicelle method and batch method. The thin (< 2 mm high) plates have exquisite optical properties and are well suited for the detection of microcrystals and for birefringence-free imaging between crossed polarizers. The plates allow for in meso crystallization trials with 50 nanoliters protein/lipid mesophase and 1 microliter precipitant solution per trial.

The 96 well LCP Glass Sandwich Plate consists of a) 127.8 x 85.5 x 1 mm glass base plate with the footprint of an SBS-compliant plate, a 140 µm thick double sticky spacer with 96 punched out holes and b) a 0.2 mm thick glass coverslip. The double sticky spacer is already adhered to the base plate. A brown paper liner covers and protects the top of the double sticky spacer and base plate. The 0.2 mm thick glass coverslip fits over and seals the entire 96 well lower plate. Alternatively a series of twenty-four siliconized 18 x 18 mm No. 1 square cover slides (HR3-152) can be used to seal the entire 96 well lower plate. Each 18 x 18 mm No. 1 cover slide seals 4 wells. Space for a bar code is available at the left end of the plate. Each well can contain 50 nanoliters of cubic phase and 1 microliter of crystallization reagent.

18 x 18 mm No. 1 Siliconized Cover Slides are made from chemically resistant borosilicate glass D 263 M of the first hydrolytic class. The slides are colorless, clear, and suitable for fluorescence microscopy. The slides feature a super hydrophobic surface on both sides. The slides are No. thickness (0.13 ro 0.16 mm). The slides are supplied in a two compartment plastic box, 100 slides per box, 10 boxes per case, 1,000 slides total for HR3-152.

The Tungsten-carbide glass cutter can be used for cutting and removal of the upper coverglass that seals the LCP Sandwich Set. Sold separately.

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LCP Sandwich Set

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LCP Sandwich Set
LCP Sandwich Set
LCP Sandwich Set
LCP Sandwich Set
LCP Sandwich Set

CAT NO

HR3-151

NAME

LCP Sandwich Set

DESCRIPTION

Pack of 20

PRICE

$458.00

cart quote

CAT NO

HR3-152

NAME

18 x 18 mm No. 1 Siliconized Cover Slides, Squares

DESCRIPTION

Case of 10 packs

PRICE

$322.00

cart quote

Support Material(s)

LCP Sandwich Set HR3-151 LCP Sandwich Set User GuideLCP Sandwich Set HR3-151 LCP Sandwich Set Dimension Drawing

Related Item(S)

  • 4 Inch Soft Rubber Brayer
  • Tungsten Carbide Scribe & Glass Cutter with Replaceable Tips

References

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

2. A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases. Vadim Cherezov, Avinash Peddi, Lalitha Muthusubramaniam, Yuan F. Zheng and Martin Caffrey. Acta Cryst. (2004). D60, 1795-1807 DOI: 10.1107/S0907444904019109.

3. Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. Faham, S. & Bowie, J. U. (2002). J. Mol. Biol. 316, 1-6.