3DQG
Peptide-binding domain of heat shock 70 kDa protein F, mitochondrial precursor, from Caenorhabditis elegans.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 90.418, 120.159, 56.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.500 - 1.720 |
| R-factor | 0.184 |
| Rwork | 0.183 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2OP6.pdb |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.575 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.600 | 1.760 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.061 | 0.551 |
| Number of reflections | 63652 | |
| <I/σ(I)> | 11.4 | 1.92 |
| Completeness [%] | 95.6 | 64.3 |
| Redundancy | 6.6 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.2 M ammonium sulfate, 20% PEG-4000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
