1DM9
HEAT SHOCK PROTEIN 15 KD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 160 |
Detector technology | IMAGE PLATE |
Collection date | 1997-09-01 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 113.070, 67.930, 41.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.226 |
Rwork | 0.226 |
R-free | 0.28560 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.608 |
Data reduction software | bioteX |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.051 | 0.353 |
Number of reflections | 21673 | 1911 * |
<I/σ(I)> | 7.23 | |
Completeness [%] | 98.4 | 88.9 |
Redundancy | 5 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 298 | drop consists of equal volume of protein and precipitant solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 11 (mg/ml) | |
2 | 1 | drop | 20 (mM) | ||
3 | 1 | drop | EDTA | 1 (mM) | |
4 | 1 | drop | HEPES | 50 (mM) | |
5 | 1 | reservoir | ammonium sulfate | 2.0 (M) | precipitant |
6 | 1 | reservoir | sodium acetate | 0.1 (M) | precipitant |
7 | 1 | reservoir | glycerol | 10 (%) | precipitant |