1PEV
Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9A |
Synchrotron site | NSLS |
Beamline | X9A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-10-14 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.98 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.660, 90.817, 76.983 |
Unit cell angles | 90.00, 94.06, 90.00 |
Refinement procedure
Resolution | 21.700 * - 2.000 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nr0 |
RMSD bond length | 0.008 |
RMSD bond angle | 26.900 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.700 * | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.058 | 0.256 |
Number of reflections | 36740 | |
Completeness [%] | 97.0 | 87.8 * |
Redundancy | 2.97 | 2.48 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 * | 289 | PEG 8000, MES, manganese chloride, glycerol, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3-4 (mg/ml) | |
2 | 1 | reservoir | MES | 0.1 (M) | |
3 | 1 | reservoir | PEG8000 | 20 (%) | |
4 | 1 | reservoir | 10 (mM) | ||
5 | 1 | reservoir | glycerol | 3 (%) | pH6.0 |