3O47
Crystal structure of ARFGAP1-ARF1 fusion protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-05-11 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | I 21 21 21 |
| Unit cell lengths | 79.298, 129.161, 157.685 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.650 - 2.800 |
| R-factor | 0.2072 |
| Rwork | 0.206 |
| R-free | 0.24330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 1HUR 3dwd |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.080 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER-TNT (BUSTER 2.8.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 6.030 | 2.800 |
| Rmerge | 0.116 | 0.038 | 0.990 |
| Number of reflections | 20250 | ||
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 99.9 | 99.7 | 99.8 |
| Redundancy | 4.9 | 4.7 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 291 | 20% PEG-3350, 0.2M trilithium sulfate, pH not applicable, vapor diffusion, temperature 291K |






