2CI9
Nck1 SH2-domain in complex with a dodecaphosphopeptide from EPEC protein Tir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-06-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.092, 60.518, 65.061 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.020 - 1.500 |
| R-factor | 0.198 |
| Rwork | 0.196 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NCK1-APO |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.171 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.040 | 0.310 |
| Number of reflections | 38419 | |
| <I/σ(I)> | 28.1 | 4.2 |
| Completeness [%] | 96.4 | 88 |
| Redundancy | 4 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | TECHNIQUE: HANGING-DROP, VAPOR-DIFFUSION PROTEIN CONCENTRATION: 8MG/ML PROTEIN:LIGAND = 1:1.1 RESERVOIRE: 2.4M (NH4)2HPO4, 0.1M TRIS, PH 8.5 CRYOCONDITIONS: 50% MPD |
