2IV8
beta appendage in complex with b-arrestin peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-09-01 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.952, 35.484, 190.624 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.780 - 2.800 |
R-factor | 0.22 |
Rwork | 0.213 |
R-free | 0.36900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e42 CHAIN A |
RMSD bond length | 0.023 |
RMSD bond angle | 2.246 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.780 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.060 | 0.150 |
Number of reflections | 4759 | |
<I/σ(I)> | 8.7 | 5 |
Completeness [%] | 70.5 | 63.5 |
Redundancy | 5 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.4 | 0.2M MG FORMATE 30% PEG 3350 OTHER REMARKS: THIS WAS THE ONLY CRYSTAL OBTAINED DESPITE HEROIC ATTEMPTS. THE CRYSTAL WAS HIGHLY MOSAIC, AND EPITAXIALLY SPLIT, LIMITING THE AMOUNT OF DATA WHICH COULD BE COLLECTED., pH 7.40 |