FRAP (Fluorescence recovery after photobleaching) measures membrane protein mobility in lipids in a high throughput fashion. The system utilizes an automated high throughput LCP-FRAP assay to prescreen membrane protein crystallization conditions.
The FRAP assay can be used to pre-screen multiple protein constructs, lipids and additives to eliminate those conditions that are non-conducive to protein diffusion, and thus crystallization, from the subsequent crystallization trials. High protein mobility and fast diffusion rates correlate well with crystallization conditions.
The FRAP sandwich set consists of a base glass slide with sealing film and an optimized cover slip. This product has been developed jointly with the renowned Scripps Research Institute in La Jolla, California, USA.
The FRAP Sandwich Set is optimized for the pre-crystallization study of membrane proteins.
Developed at the NIH Roadmap Center for membrane protein research and routinely used in GPCR structural biology.
Bottom Slide Features
• Dimensions: approx 127.8 x 85.5 mm, thickness approx. 1 mm
• Superhydrophobic glass surface
• Covered with a 0.06 mm (60 micron) high spacer. This spacer has 96 recesses of 5 mm diameter. They are consistent with the SBS format for robotic handling. The spacer has an adhesive surface to which the hydrophobic coverslip attaches. The crystallization drops are, hence, sealed in these reaction chambers.
Cover Slip Features
• Dimensions: approx 112 x 77 mm, thickness No. 1.5 (0.16 to 0.19 mm)
• Superhydrophobic glass surface
• Optimized for bright field, UV and fluorescent microscopy
The FRAP Sandwich Set is compatible with the Formulatrix FRAP.
The FRAP Sandwich Set consists of 20 Superhydrophobic Cover Slips and 20 Superhyrophobic Bottom Slides with applied sealing film.