3F1L
The 0.95 A structure of an oxidoreductase, yciK from E.coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-26 |
| Detector | MAR CCD 300 mm |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.871, 66.803, 65.053 |
| Unit cell angles | 90.00, 109.03, 90.00 |
Refinement procedure
| Resolution | 34.136 - 0.950 |
| R-factor | 0.171 |
| Rwork | 0.171 |
| R-free | 0.19200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3f1k ycik structure at 2.6A resolution solved by MAD and SAD phasing |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.915 |
| Data scaling software | d*TREK |
| Phasing software | PHENIX |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.240 | 45.240 | 0.980 |
| High resolution limit [Å] | 0.950 | 2.050 | 0.950 |
| Rmerge | 0.062 | 0.035 | 0.385 |
| Total number of observations | 104905 | 105870 | |
| Number of reflections | 236813 | ||
| <I/σ(I)> | 8.9 | 31.1 | 2.8 |
| Completeness [%] | 86.7 | 85.4 | 80.9 |
| Redundancy | 4.44 | 4.33 | 4.54 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1M HEPES pH 7.5, 0.1M sodium nitrate, 16 % w/v polyethylene glycol 8000, vapor diffusion, hanging drop, temperature 295K |
