2Z5L
The first ketoreductase of the tylosin PKS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2007-03-08 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.116 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.180, 49.810, 68.810 |
| Unit cell angles | 90.00, 109.20, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.950 |
| R-factor | 0.259 |
| Rwork | 0.259 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2FR0.pdb |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.046 | 0.381 |
| Number of reflections | 28533 | |
| <I/σ(I)> | 19.6 | 1.7 |
| Completeness [%] | 93.4 | 61.4 |
| Redundancy | 6.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 1.5M ammonium sulfate, 0.1M Tris (pH 8.0), 1:1 protein to well solution, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
