3LDN
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-02-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.830, 75.222, 89.649 |
| Unit cell angles | 90.00, 99.18, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.200 |
| R-factor | 0.20014 |
| Rwork | 0.194 |
| R-free | 0.27620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fzf |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.636 |
| 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] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.096 | 0.336 |
| Number of reflections | 36490 | |
| <I/σ(I)> | 18.3 | 3.3 |
| Completeness [%] | 97.0 | 88.8 |
| Redundancy | 2.9 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.1M Tris buffer, 25% Peg3350, 0.1M Na,K tartrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
