2OP6
Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-12 |
| Detector | SBC-3 |
| Wavelength(s) | 0.97970 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.172, 26.688, 60.995 |
| Unit cell angles | 90.00, 115.14, 90.00 |
Refinement procedure
| Resolution | 30.440 - 1.850 |
| R-factor | 0.1735 |
| Rwork | 0.169 |
| R-free | 0.21240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yuw |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.555 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.440 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.072 | 0.334 |
| Number of reflections | 12530 | |
| <I/σ(I)> | 15.1 | 1.97 |
| Completeness [%] | 91.6 | 55.2 |
| Redundancy | 3.2 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 1.4 M Tri-sodium citrate, 0.1 M HEPES buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
