1PGU
YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-01-02 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97902,0.918,0.97932 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.800, 154.530, 69.000 |
Unit cell angles | 90.00, 90.65, 90.00 |
Refinement procedure
Resolution | 25.000 * - 2.300 |
R-factor | 0.202 |
Rwork | 0.202 |
R-free | 0.25700 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 26.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.440 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.069 * | 0.230 * |
Total number of observations | 192792 * | |
Number of reflections | 51350 * | |
Completeness [%] | 90.9 * | 93.1 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 15% PEG 4000, 100mM NaCl, 100mM Hepes, pH 7.5, 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 | HEPES | 100 (mM) | pH7.5 |
3 | 1 | reservoir | 200 (mM) | ||
4 | 1 | reservoir | PEG4000 | 13 (%(w/v)) |