1IAP
CRYSTAL STRUCTURE OF P115RHOGEF RGRGS DOMAIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-01-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9760 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.859, 37.432, 128.171 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.550 - 1.900 |
| R-factor | 0.219 |
| Rwork | 0.219 |
| R-free | 0.27500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SE-MET STRUCTURE OF THE SAME PROTEIN SOLVED BY MAD PHASING FROM A FOUR-WAVELENGTH MAD DATASET COLLECTED AT CHESS F2 BEAMLINE (UNPUBLISHED DATA) |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.000 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 16.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.120 | 0.485 |
| Number of reflections | 13303 | |
| <I/σ(I)> | 12.1 | 4.8 |
| Completeness [%] | 90.0 | 79.6 |
| Redundancy | 3.8 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 9.5 | 20 * | PEG 3350, ammonium formate, CHES, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG3350 | 18-22 (%(w/v)) | |
| 2 | 1 | reservoir | CHES | 83 (mM) | |
| 3 | 1 | reservoir | ammonium formate | 80-240 (mM) |
