The CALIXAR™ v2.0 Additive Kit


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The CALIXAR™ v2.0 Additive Kit


New reagents have been designed to structure the membrane domains through hydrophobic interactions and a network of salt bridges with the basic residues found at the cytosol-membrane interface of membrane proteins.

These reagents behave as surfactants forming micelles of 5–24 nm, with the critical micellar concentration (CMC) ranging from 0.05 to 1.5 mM, although sensitive to pH. Such molecules were successfully used to promote crystallization of membrane proteins.

Crystals of  a 12TM transporter grown in A. CALX153ACE and B. CALX113ACE using vapour diffusion. Images provided courtesy of Arnaud KILBURG and Pierre FALSON. Structure image courtesy of Prof. Peter Crowley at the National University of Ireland, Galway.

These examples illustrate that these additives can promote membrane protein crystallization and help to obtain diffracting protein crystals.

Features of The CALIXAR™ v2.0 Additive Kit:
  • Promotes crystallization of functional membrane proteins
  • Generates a saltbridge network around the protein and hydrophobic contacts

This product is manufactured and distributed under an exclusive license using CALIXAR™ patented technology and is supplied for research use only.
This product may not be used for the provision of commercial services for which a separate license must be obtained.

The CALIXAR™ v2.0 Additive Kit 24 x 50 μL MD1-95 The CALIXAR™ v2.0 Additive Kit Single Reagent 50 μL MDSR-95- CALIXAR™ single reagents are manufactured by Calixar SAS and exclusively licensed to Molecular Dimensions for the manufacture and distribution of this additive kit for final end users only. The use of this kit for commercial service purposes requires a separate license from Calixar SAS.


Matar Merheb M et al., PLoSONE 2011
McGovern et al.Nat, Chem. 2012, 4, 527-533. Protein camouflage in cytochrome c-calixarene complexes.
McGovern et al. Chem. Commun. 2014, 50, 10412-10415. Protein assembly mediated by sulfonatocalix[4]arene.
McGovern et al. Chem. Sci. 2015, 6, 442-449. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme.

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