1OEB
Mona/Gads SH3C domain
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 28.691, 72.072, 34.168 |
| Unit cell angles | 90.00, 97.70, 90.00 |
Refinement procedure
| Resolution | 36.040 * - 1.700* |
| R-factor | 0.174 |
| Rwork | 0.171 |
| R-free | 0.21940 * |
| Structure solution method | MAD |
| RMSD bond length | 0.012 * |
| RMSD bond angle | 1.375 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.000 | 1.750 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.055 | 0.404 |
| Total number of observations | 99470 * | |
| Number of reflections | 15317 | |
| <I/σ(I)> | 28.2 | 4 |
| Completeness [%] | 98.2 * | 81.4 |
| Redundancy | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.5 | 20 * | PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG4000 | 20 (%) | |
| 2 | 1 | reservoir | 5 (mM) | ||
| 3 | 1 | reservoir | sodium cacodylate | 50 (mM) | pH6.5 |
| 4 | 1 | drop | protein | 10 (mg/ml) |
