1LP1
Protein Z in complex with an in vitro selected affibody
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-10-01 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.098 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 55.546, 55.546, 155.749 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.225 |
| Rwork | 0.224 |
| R-free | 0.25500 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Polyserine model of PDB entry 1DEE chain G |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.170 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.050 | 0.290 * |
| Total number of observations | 57198 * | |
| Number of reflections | 6847 * | |
| Completeness [%] | 99.7 * | 99.8 |
| Redundancy | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 * | 298 | MgSO4, MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 72 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.5 |
| 3 | 1 | reservoir | 1.6 (M) | ||
| 4 | 1 | reservoir | MES | 100 (mM) | pH6.5 |
