4QT7
Crystal structure of the c-Src SH3 domain in complex with a peptide from the Hepatitis C virus NS5A-protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-11-28 |
| Wavelength(s) | 0.93340 |
| Spacegroup name | I 41 |
| Unit cell lengths | 62.307, 62.307, 27.266 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.979 - 1.550 |
| R-factor | 0.1605 |
| Rwork | 0.159 |
| R-free | 0.19450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jz4 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.263 |
| Data scaling software | Aimless (0.2.17) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 24.980 | 24.980 | 1.580 |
| High resolution limit [Å] | 1.550 | 8.490 | 1.550 |
| Rmerge | 0.091 | 0.044 | 0.489 |
| Rpim | 0.012 | 0.386 | |
| Total number of observations | 642 | 801 | |
| Number of reflections | 14570 | ||
| <I/σ(I)> | 23.7 | 54.4 | 2.3 |
| Completeness [%] | 98.2 | 97.2 | 82.8 |
| Redundancy | 9.6 | 11.7 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 2M Ammonium sulphate, 0.1M sodium chloride, 0.86mM methyl-beta-cyclodextrin, 0.1M Hepes, pH 7, vapor diffusion, hanging drop, temperature 298K |
