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Expressing Crystal-Quality Proteins with LEXSY

(1) LEXSY – Crystal Quality Proteins

Crystallization of proteins and subsequent X-ray diffraction has been the major source for high resolution protein structures for decades. While the art of protein crystallization is a science of its own, in many cases the actual quality of the protein to be crystallized (coming from expression/purification) is pivotal for obtaining X-ray suitable crystals.

The eukaryotic expression system LEXSY is becoming increasingly popular with crystallographers since it

  • shows high expression success rates (> 90 %) for eukaryotic proteins for which many other systems fail
  • produces homogeneously glycosylated proteins being prone for crystallization
  • allows simple amino acid isotope labeling[1,2]
Crystal structures for human N-acetyl serotonin methyltransferase, Cu/Zn superoxide dismutase and  legumain have all been determined using LEXSY-proteins.
Figure 1: Crystal structures for human N-acetyl serotonin methyltransferase, Cu/Zn superoxide dismutase and legumain have all been determined using LEXSY-proteins.[3–5]
Left: Structure of human N-acetyl serotonin methyltransferase dimer.[3] Right: Crystal of human legumain.[4]




(2) LEXSY – all you need to get started

LEXSY Expression Kits
Convenient all-in-one expression kits allowing constitutive or inducible, intracellular or secretory expression of target proteins. This is the place to start if you are new to LEXSY.

LEXSY Strains & Cultivation Kits
The LEXSY expression hosts, as strains or complete ready-to-grow cultivation kits.

LEXSY Cultivation Media
Complex and synthetic media for optimal growth of LEXSY strains.

LEXSY Antibiotics
For efficient selection of recombinant strains.

LEXSY Expression Vectors
Available with six different selection markers.

PCR and Cloning enzymes
All restriction enzymes for the pLEXSY cloning sites, ligases, polymerases etc.

Need further information? Please check out the LEXSY section at the Jena Bioscience website!
Or contact us by email at: expression@jenabioscience.com


References:

[1] Niculae et al. (2006) Isotopic labeling of recombinant proteins expressed in the protozoan host Leishmania tarentolae. Protein Expr. Purif. 48:167.

[2] Foldynová-Trantirková et al. (2009) A cost-effective amino-acid-type selective isotope labeling of proteins expressed in Leishmania tarentolae. J. Biomol. Struct. Dyn. 26:755.

[3] Botros et al. (2013) Crystal structure and functional mapping of human ASMT, the last enzyme of the melatonin synthesis pathway. J. Pineal Res. 54:46.

[4] Dall and Brandstetter (2012) Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 68:24.

[5] Gazdag et al. (2010) Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 66:871.



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