3LDL
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP
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 | 2007-03-20 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9730 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.985, 74.326, 90.260 |
| Unit cell angles | 90.00, 98.81, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.300 |
| R-factor | 0.19776 |
| Rwork | 0.194 |
| R-free | 0.27852 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fzf |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.532 |
| 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 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.110 | 0.427 |
| Number of reflections | 30393 | |
| <I/σ(I)> | 10 | 2.8 |
| Completeness [%] | 92.5 | 87.7 |
| Redundancy | 2.5 | 2 |
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 |
