3QIJ
Primitive-monoclinic crystal structure of the FERM domain of protein 4.1R
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-27 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.98322 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.001, 53.469, 88.766 |
| Unit cell angles | 90.00, 106.96, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.209 |
| Rwork | 0.207 |
| R-free | 0.26150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gg3 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.464 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.055 | 0.024 | 0.989 |
| Number of reflections | 51901 | ||
| <I/σ(I)> | 10.5 | ||
| Completeness [%] | 99.7 | 98.6 | 97.1 |
| Redundancy | 3.6 | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 25% PEG3350, 0.2M magnesium chloride, 1% w/w dispase-I, pH 7.5, vapor diffusion, sitting drop, temperature 293K |
