1GPQ
Structure of ivy complexed with its target, HEWL
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Collection date | 2000-08-15 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.490, 59.560, 69.200 |
| Unit cell angles | 90.00, 95.39, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.600 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.21200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hel |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.650 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.044 | 0.131 |
| Number of reflections | 58982 | |
| <I/σ(I)> | 6.7 | 4.1 |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 3.4 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 15% PEG 4000, 5% GLYCEROL, CHES BUFFER 0.1M PH 9.0, PROTEIN CONCENTRATION: 5MG.ML-1 |
