1ELW
Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-10-02 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 41 |
| Unit cell lengths | 75.470, 75.470, 42.890 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.870 - 1.600 |
| R-factor | 0.18 |
| Rwork | 0.180 |
| R-free | 0.21500 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.300 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.041 | 0.305 |
| <I/σ(I)> | 32.5 | |
| Completeness [%] | 95.8 | 75.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | used to microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein-peptide complex | 20 (mg/ml) | |
| 2 | 1 | drop | HEPES | 15 (mM) | |
| 3 | 1 | reservoir | Tris | 100 (mM) | |
| 4 | 1 | reservoir | PEG2000 MME | 24 (%(w/v)) | |
| 5 | 1 | reservoir | 10 (mM) | ||
| 6 | 1 | reservoir | xylitol | 15 (%(w/v)) |






