3GGF
Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-01-30 |
| Detector | MAR225 CCD |
| Wavelength(s) | 0.8800 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.920, 91.250, 108.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.780 - 2.350 |
| R-factor | 0.22168 |
| Rwork | 0.219 |
| R-free | 0.27698 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ckx |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.477 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0085) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.780 | 2.480 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.139 | 0.849 |
| Number of reflections | 28094 | |
| <I/σ(I)> | 9 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 277.15 | 12%w/v PEG 3350; 0.005M CdCl2; 0.1M HEPES, pH7.0 , VAPOR DIFFUSION, SITTING DROP, temperature 277.15K |
