3VRN
Crystal structure of the tyrosine kinase binding domain of Cbl-c
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2007-06-25 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.900 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 93.223, 107.617, 54.773 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.240 - 1.640 |
| R-factor | 0.1834 |
| Rwork | 0.182 |
| R-free | 0.21770 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cbl |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.849 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.670 |
| High resolution limit [Å] | 1.640 | 4.450 | 1.640 |
| Rmerge | 0.054 | 0.027 | 0.446 |
| Number of reflections | 34203 | ||
| <I/σ(I)> | 27.992 | 50.879 | 3.452 |
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 4.3 | 4.1 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 16% PEG3350, 0.1M ammonium formate, 0.2M NDSB-201, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
