1NF3
Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-03-08 |
| Detector | SBC-2 |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 |
| Unit cell lengths | 41.744, 53.787, 79.521 |
| Unit cell angles | 81.55, 76.59, 90.04 |
Refinement procedure
| Resolution | 30.000 * - 2.100 |
| R-factor | 0.219 |
| Rwork | 0.219 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ngr |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.200 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.500 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.104 | 0.500 |
| Total number of observations | 80223 * | |
| Number of reflections | 38985 | |
| <I/σ(I)> | 9.2 | 2 |
| Completeness [%] | 89.6 | 87.1 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | 20 * | 24% PEG 4000, 100mM sodium citrate, 0.2M ammonium acetate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 20 (mM) | pH8.5 |
| 3 | 1 | drop | 1 (mM) | ||
| 4 | 1 | drop | GMPPNP | 0.100 (mM) | |
| 5 | 1 | drop | beta-mercaptoethanol | 10 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 24 (%) | |
| 7 | 1 | reservoir | sodium citrate | 100 (mM) | pH6.4 |
| 8 | 1 | reservoir | ammonium acetate | 0.2 (M) |
