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JBScreen Classic

JBScreen Classic is a crystallization kit designed for efficient and flexible screening of crystallization conditions for proteins, peptides, nucleic acids, macromolecular complexes and water-soluble small molecules.

The JBScreen Classic Kits 1-10 cover 240 of the most prominent buffers for protein crystallization. Their compositions result from data mining of several thousands of crystallized proteins. JBScreen Classic represents the statistically most successful buffers that yielded protein crystals suitable for X-ray diffraction.

The JBScreen Classic buffers are principally ordered by type and concentration of the precipitant. This allows easy extraction of all relevant information and is already a first step to a refinement: Once you get a hit, you immediately see the effects of the neighbouring conditions. Subsequent fine tuning of preliminary hits will be much more efficient.

JBScreen Classic comprises 10 kits of 24 unique reagents in the standard 10 ml bulk format.

JBScreen Classic HTS I+II contains the formulations of the JBScreen system, adopted to fit the 96-well format for high throughput crystallization applications. Each JBScreen Classic HTS deep-well block is pre-filled with 96 sterile conditions at 1.7 ml each.

 

Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.

BIOZ Product Citations

Please click the arrow on the right to expand the citation list. Click publication title for the full text.


Further Selected Literature Citations of JBScreen Classic

  • Zannini et al. (2022) Structural Insights into a Fusion Protein between a Glutaredoxin-like and a Ferredoxin-Disulfide Reductase Domain from an Extremophile Bacterium. Inorganics 10(2):24.
  • Mwangangi et al. (2021) The structure of the actin filament uncapping complex mediated by twinfilin. Science Advances 7:eabd5271.
  • Sánchez-Ruiz et al. (2021) Agaricales Mushroom Lignin Peroxidase: From Structure–Function to Degradative Capabilities. Antioxidants 10:1446.
  • Ferrero et al. (2021) Snapshots of a Non‐Canonical RdRP in Action. Viruses 13:1260.
  • Ferrero et al. (2021) Structure and Double-Stranded RNA-Binding Activity of the Birnavirus Drosophila X Virus VP3 Protein. Journal of Virology 95(4):e02166-20.
  • Dolot et al. (2021) Biochemical, crystallographic and biophysical characterization of histidine triad nucleotide-binding protein 2 with different ligands including a non-hydrolyzable analog of Ap4A. BBA - General Subjects 1865(11):129968.
  • Taudte et al. (2021) Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis. JBC 296:100263.
  • Bretagne et al. (2021) Crystal structure of Dictyoglomus thermophilum β-D-xylosidase DtXyl unravels the structural determinants for efficient notoginsenoside R1 hydrolysis. Biochimie 181:34.
  • Cheng et al. (2021) Crystal structure of the GTP-binding protein-like domain of AGAP1. Acta Cryst F 77:105.
  • Chen et al. (2021) Purification, crystallization, and X-ray diffraction analysis of myocyte enhancer factor 2D and DNA complex. Protein Expression and Purification 179:105788.
  • Giunta et al. (2020) Tuning the Properties of Natural Promiscuous Enzymes by Engineering Their Nano-environment. ACS Nano 14:17652.
  • Garcia-Rodriguez et al. (2020) The Escherichia coli RnlA–RnlB toxin–antitoxin complex: production, characterization and crystallization. Acta Cryst F 76:31.
  • Sheu-Gruttadauria et al. (2019) Beyond the seed: structural basis for supplementary microRNA targeting by human Argonaute2. The EMBO Journal e101153.
  • Pozzi et al. (2019) Evidence of Destabilization of the Human Thymidylate Synthase (hTS) Dimeric Structure Induced by the Interface Mutation Q62R. Biomolecules DOI:10.3390/biom9040134.
  • Deka et al. (2018) Structural and biochemical studies on the role of active site Thr166 and Asp236 in the catalytic function of D-Serine deaminase from Salmonella typhimurium. Biochem. Biophys. Res. Commun. 504:40.
  • Dall et al. (2018) Structural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril states. J. Biol. Chem. 293:13151.
  • Rinaldi et al. (2018) Crystallization and initial X-ray diffraction analysis of the multi-domain Brucella blue light-activated histidine kinase LOV-HK in its illuminated state. Biochem. Biophys. Rep. 16:39.
  • Flores-Ibarra et al. (2018) Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail. Sci. Rep. 8:9835.
  • Bernedo-Navarro et al. (2018) Structural Basis for the Specific Neutralization of Stx2a with a Camelid Single Domain Antibody Fragment. Toxins 10:108.