1UIX
Coiled-coil structure of the RhoA-binding domain in Rho-kinase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-18B |
Synchrotron site | Photon Factory |
Beamline | BL-18B |
Temperature [K] | 93 |
Detector technology | DIFFRACTOMETER |
Collection date | 1999-12-15 |
Detector | WEISSENBERG |
Wavelength(s) | 0.9784, 0.9778, 0.9600, 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 148.000, 26.100, 39.600 |
Unit cell angles | 90.00, 90.40, 90.00 |
Refinement procedure
Resolution | 39.500 - 1.800 |
R-factor | 0.219 |
Rwork | 0.193 |
R-free | 0.23600 |
Structure solution method | MAD |
RMSD bond length | 0.018 * |
RMSD bond angle | 1.511 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.530 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.045 | 0.082 |
Total number of observations | 139215 * | |
Number of reflections | 12896 | |
<I/σ(I)> | 18.2 | 14.8 |
Completeness [%] | 89.0 | 68.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | Thara, K., (2000) Acta Crystallogr., D56, 1042. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.7 (mg/ml) | |
2 | 1 | drop | HEPES | 55 (mM) | pH7.0 |
3 | 1 | drop | 23 (mM) | ||
4 | 1 | drop | PEG1000 | 11 (%) | |
5 | 1 | drop | ethylene glycol | 14 (%) | |
6 | 1 | drop | n-octanoylsucrose | 22 (mM) | |
7 | 1 | reservoir | HEPES | 100 (mM) | pH7.0 |
8 | 1 | reservoir | PEG1000 | 25 (%) | |
9 | 1 | reservoir | ethylene glycol | 30 (%) |