1QUU
CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02-10 |
| Detector | OFF-LINE SCANNER |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 60.050, 60.050, 390.810 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 2.500 |
| R-factor | 0.2285 |
| Rwork | 0.229 |
| R-free | 0.31050 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.272 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.062 | 0.339 |
| Number of reflections | 21275 | |
| <I/σ(I)> | 15.3 | |
| Completeness [%] | 94.6 | 89.8 |
| Redundancy | 6.1 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.4 * | 277 | 26% PEG 400 (FLUKA), 100 MM MGSO4, 100 MM HEPES OR TRIS-HCL, pH 7.5, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 150 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | DTT | 1 (mM) | |
| 4 | 1 | reservoir | PEG400 | 26 (%) | |
| 5 | 1 | reservoir | 100 (mM) | ||
| 6 | 1 | reservoir | HEPES | 100 (mM) | can be replaced by Tris-HCl |
