3O5W
Binding of kinetin in the active site of mistletoe lectin I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-07 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.8162 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 107.573, 107.573, 310.633 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.970 - 2.700 |
| R-factor | 0.17669 |
| Rwork | 0.174 |
| R-free | 0.22586 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m2t |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.049 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 7.220 | 2.700 |
| Rmerge | 0.139 | 0.036 | |
| Number of reflections | 30058 | ||
| <I/σ(I)> | 6.1 | ||
| Completeness [%] | 99.3 | 99.1 | 99 |
| Redundancy | 8.9 | 7.9 | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | COUNTER-DIFFUSION | 2.5 | 293 | 1.0M ammonium sulphate, 0.2M glycine/HCl, pH 2.5, counter diffusion, temperature 293K |
