3KEN
Human Eg5 in complex with S-trityl-L-cysteine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-08-13 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.5418 |
Spacegroup name | I 21 3 |
Unit cell lengths | 157.930, 157.930, 157.930 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.500 |
Rwork | 0.241 |
R-free | 0.27500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1X88 molecule A |
RMSD bond length | 0.008 |
RMSD bond angle | 1.427 |
Data reduction software | SAINT |
Data scaling software | PROTEUM PLUS (PLUS) |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.780 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 22664 | |
<I/σ(I)> | 14.18 | 2.89 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.92 | 6.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | 250 mM NH4SO4, 100 mM MES pH 6.0, 25% PEG 3350, 5-15% glycerol, 10 mM trimethylamine, VAPOR DIFFUSION, SITTING DROP, temperature 277K |