4FCM
Crystal structure of the NTF2-like domain of human G3BP1 in complex with a peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-09 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.04 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.780, 71.490, 89.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.380 - 2.690 |
| R-factor | 0.2277 |
| Rwork | 0.225 |
| R-free | 0.28220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fcj |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.589 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.380 | 2.760 |
| High resolution limit [Å] | 2.690 | 2.690 |
| Rmerge | 0.129 | 0.943 |
| Number of reflections | 7987 | |
| <I/σ(I)> | 10 | 1.8 |
| Completeness [%] | 99.3 | 99.9 |
| Redundancy | 3.9 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 279 | 20% PEG3350, 0.1 M Bis-tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 279K |






