3NF1
Crystal structure of the TPR domain of kinesin light chain 1
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 | 2009-09-18 |
| Detector | MAR-300 |
| Wavelength(s) | 0.92015 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 74.685, 74.685, 156.168 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.880 - 2.800 |
| R-factor | 0.204 |
| Rwork | 0.200 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ceq |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.8.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 6.020 | 2.800 |
| Rmerge | 0.068 | 0.039 | 0.584 |
| Number of reflections | 12665 | ||
| <I/σ(I)> | 15.7 | ||
| Completeness [%] | 97.2 | 99.4 | 78.7 |
| Redundancy | 8.6 | 9.4 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 2.0M ammonium formate, 0.1M HEPES, 0.001M TCEP., pH 7.5, vapor diffusion, sitting drop, temperature 291K |






