1G4R
CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-05-24 |
| Detector | BRANDEIS - B4 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 77.806, 77.806, 157.099 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.940 - 2.200 |
| R-factor | 0.238 |
| Rwork | 0.238 |
| R-free | 0.26700 * |
| Structure solution method | MOLECULAR REPLACEMENT, SHARP |
| Starting model (for MR) | 1cf1 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.046 | 0.456 * |
| Total number of observations | 267488 * | |
| Number of reflections | 27920 * | |
| <I/σ(I)> | 10.3 | 1.4 |
| Completeness [%] | 94.7 * | 79.2 * |
| Redundancy | 9.6 * | 3.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 8.5 * | 19 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 5 (mg/ml) | or 7mg/ml |
| 2 | 1 | 1 | 0.1 (M) | ||
| 3 | 1 | 1 | Tris-HCl | 20 (mM) | |
| 4 | 1 | 1 | EDTA | 1 (mM) | |
| 5 | 1 | 1 | dithiothreitol | 10 (mM) | |
| 6 | 1 | 1 | glycerol | 5 (%) | |
| 7 | 1 | 2 | PEG1500 | 18-20 (%) | |
| 8 | 1 | 2 | 0.8 (M) | ||
| 9 | 1 | 2 | Tris-HCl | 0.1 (M) |
