4NFM
Human tau tubulin kinase 1 (TTBK1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-01-15 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.9797 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 170.300, 39.900, 50.400 |
| Unit cell angles | 90.00, 104.30, 90.00 |
Refinement procedure
| Resolution | 47.480 - 2.120 |
| R-factor | 0.2058 |
| Rwork | 0.204 |
| R-free | 0.24090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cki |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.060 |
| Data reduction software | HKL-2000 ((DENZO)) |
| Data scaling software | HKL-2000 ((SCALEPACK)) |
| Phasing software | AMoRE |
| Refinement software | BUSTER-TNT (BUSTER 2.11.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.210 |
| High resolution limit [Å] | 2.120 | 2.120 |
| Rmerge | 0.070 | 0.490 |
| Number of reflections | 18769 | |
| <I/σ(I)> | 17.3 | 2.7 |
| Completeness [%] | 99.4 | 100 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 100 mM Ammonium Acetate, pH 7.0, 19% (w/v) PEG5000 (methyl ester), 100 mM Ammonium Acetate, unbuffered, vapor diffusion, hanging drop, temperature 277K |
