1S3X
The crystal structure of the human Hsp70 ATPase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 120 |
Detector technology | AREA DETECTOR |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 145.470, 63.340, 45.950 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.840 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1atr |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.260 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 6.000 | 1.890 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.049 | 0.020 |
Number of reflections | 35081 | 3392 * |
<I/σ(I)> | 28.3 | |
Completeness [%] | 95.5 | 94.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 10 * | imidazole buffer, PEG 8000, CaCl2, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | reservoir | imidazole | 25 (mM) | pH7.0 |
3 | 1 | reservoir | PEG8000 | 8 (%) | |
4 | 1 | reservoir | 20 (mM) | ||
5 | 1 | reservoir | gamma-S-ATP | 1 (mM) |