1P8Z
Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-07 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0052 |
Spacegroup name | P 31 1 2 |
Unit cell lengths | 114.220, 114.220, 93.770 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.26300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.580 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.077 * | 0.267 * |
Number of reflections | 21012 | 2115 * |
Completeness [%] | 97.4 | 99.2 |
Redundancy | 3.6 * | 3.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 20 * | 0.1M Sodium Acetate, 10 mM Cadmium Chloride, 12.5% (v/v) PEG 400, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG400 | 12.5 (%(v/v)) | |
3 | 1 | reservoir | 0.1 (M) | pH5.0 | |
4 | 1 | reservoir | 10 (mM) |