4X9L
N-terminal domain of Heat shock protein 90 from Oryza sativa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-25 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.953725 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 116.870, 116.870, 105.340 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.416 - 3.100 |
R-factor | 0.2475 |
Rwork | 0.245 |
R-free | 0.29170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2jki |
RMSD bond length | 0.009 |
RMSD bond angle | 1.453 |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 58.440 | 3.270 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.133 | 0.836 |
Number of reflections | 6890 | |
<I/σ(I)> | 12.8 | 3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11 | 11.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 290 | 0.1M Tris, PEG 400, Ammonium sulphate |