FRAP

Resources

Publications
2017

Methods used to study the oligomeric structure of G-protein-coupled receptors

Guo H, An S, Ward R, et al. Methods used to study the oligomeric structure of G-protein-coupled receptors. Bioscience Reports. 2017;37(2):BSR20160547. doi:10.1042/BSR20160547.
  
2015
Salom D, Padayatti PS, Palczewski K. Crystallization of G Protein-Coupled Receptors. Methods in cell biology. 2013;117:451-468. doi:10.1016/B978-0-12-408143-7.00024-4.
 
Gustavo Fenalti, Enrique E. Abola, Chong Wang, Beili Wu, Vadim Cherezov, Chapter Twenty - Fluorescence Recovery After Photobleaching in Lipidic Cubic Phase (LCP-FRAP): A Precrystallization Assay for Membrane Proteins, Editor(s): Arun K. Shukla, In Methods in Enzymology, Academic Press, Volume 557, 2015, Pages 417-437, ISSN 0076-6879, ISBN 9780128021835, https://doi.org/10.1016/bs.mie.2014.12.008.
 
Milić D, Veprintsev DB. Large-scale production and protein engineering of G protein-coupled receptors for structural studies. Frontiers in Pharmacology. 2015;6:66. doi:10.3389/fphar.2015.00066.
 
2014
Xin Yin, Henghao Xu, Michael Hanson and Wei Liu, GPCR Crystallization Using Lipidic Cubic Phase Technique, Current Pharmaceutical Biotechnology, volume 15, issue 10, pages 971-979, year 2014, issn 1389-2010/1873-4316, doi 10.2174/1389201015666140922110325
 
2013
Siu FY, He M, de Graaf C, et al. Structure of the class B human glucagon G protein coupled receptor. Nature. 2013;499(7459):10.1038/nature12393. doi:10.1038/nature12393.
 
2012
Stevens RC, Cherezov V, Katritch V, et al. GPCR Network: a large-scale collaboration on GPCR structure and function. Nature reviews Drug discovery. 2013;12(1):25-34. doi:10.1038/nrd3859.
 
2011
Fei Xu, Wei Liu, Michael A. Hanson, Raymond C. Stevens, and Vadim Cherezov
Crystal Growth & Design 2011 11 (4), 1193-1201
DOI: 10.1021/cg101385e
 
Joseph JS, Liu W, Kunken J, Weiss TM, Tsuruta H, Cherezov V. Characterization of Lipid Matrices for Membrane Protein Crystallization by High-Throughput Small Angle X-ray Scattering. Methods (San Diego, Calif). 2011;55(4):342-349. doi:10.1016/j.ymeth.2011.08.013.
 
Cherezov V. Lipidic Cubic Phase Technologies for Membrane Protein Structural Studies. Current opinion in structural biology. 2011;21(4):559-566. doi:10.1016/j.sbi.2011.06.007.
 
2008
Vadim Cherezov, Jeffrey Liu, Mark Griffith, Michael A. Hanson, and Raymond C. Stevens
Crystal Growth & Design 2008 8 (12), 4307-4315
DOI: 10.1021/cg800778j
Computer Requirements

The standard FRAP controlling computer offered with the instrument supports imaging with continuous multiple focus level imaging (z-slicing) and processing of all images.

FRAP uses the ROCK IMAGER control software which operates with 64-bit Windows 7 or Windows XP.

Electrical Specifications

Instrument: 100-240 VAC, 50-60 Hz, 600 W max, 1 PH

Computer: 100-240 VAC, 50-60 Hz, 525 W max, 1 PH

Temperature Regulation

System can operate in any temperature from 4° C to 30° C

Internal temperature can be controlled to within 5° C below and 7° C above ambient

Compatible Plates

SBS standard LCP plates (127.8 mm x 85.5 mm x 14.4 mm)

LCP thin glass plates (127.8 mm x 85.5 mm x 1 mm)

Physical Dimensions - FRAP Benchtop

Depth: 696 mm (28")

Width: 641 mm (26")

Height: 873 mm (35")

Weight: 70 kg (155 lbs)

Physical Dimensions - FRAP Integrated with RI1000

Depth: 1085 mm (43")

Width: 834 mm (33")

Height: 2197 mm (87")

Weight: 462 kg (1019 lb)