Crystal Screens - JBScreen Classic

JBScreen bulk & HTS

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.


Selected Recent Literature Citations of JBScreen Classic

  • Chitnumsub et al. (2014) The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities. Acta Cryst D 70:1517.
  • Serer et al. (2014) Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility. Acta Cryst D 70:1419.
  • Fernández-Fueyo et al. (2014) Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability. Biotechnology for Biofuels 7:2.
  • Chu et al. (2014) KDM4B as a Target for Prostate Cancer: Structural Analysis and Selective Inhibition by a Novel Inhibitor. J. Med. Chem. 57:5975.
  • Rosa et al. (2014) Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase. FEBS Journal DOI:10.1111/febs.12861.
  • Kolomytseva et al. (2014) Structural basis for the substrate specificity and the absence of dehalogenation activity in 2-chloromuconate cycloisomerase from Rhodococcus opacus 1CP. Biochimica et Biophysica Acta 1844:1541.
  • Morita et al. (2014) Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6. Acta Cryst F 70:794.
  • Zekiri et al. (2014) Crystallization and preliminary X-ray crystallographic analysis of polyphenol oxidase from Juglans regia (jrPPO1). Acta Cryst F 70:832.