3KMM
Structure of human LCK kinase with a small molecule inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | Cu FINE FOCUS |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-05-01 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.579, 74.160, 92.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.560 - 2.800 |
| R-factor | 0.167 |
| Rwork | 0.165 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lck |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.000 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNX (2005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.111 | 0.261 |
| Number of reflections | 7251 | |
| <I/σ(I)> | 10.4 | 3.7 |
| Completeness [%] | 94.2 | 95.7 |
| Redundancy | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 1.8-2.5M AMMONIUM SULFATE, 0.1M BISTRIS, PH6.5,VAPOR DIFFUSION, SITTING DROP, 277 DEG K, PROTEIN STOCK AT 1.5 MG/ML |
