1QPX
CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-08-25 |
| Detector | RIGAKU RAXIS |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.065, 75.442, 115.189 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.400 |
| Rwork | 0.189 |
| R-free | 0.26500 |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.397 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.069 | 0.270 |
| Total number of observations | 107688 * | |
| Number of reflections | 18542 | |
| <I/σ(I)> | 16.7 | |
| Completeness [%] | 99.3 | 93.8 |
| Redundancy | 5.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 * | 298 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | KMES | 20 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 16-22 (%) | |
| 4 | 1 | reservoir | isopropyl alcohol | 14 (%) | |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) |






