6K5Z
Structure of uridylyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 43 |
| Unit cell lengths | 73.194, 73.194, 126.036 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.330 |
| R-factor | 0.1956 |
| Rwork | 0.192 |
| R-free | 0.25490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gup |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.659 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.370 |
| High resolution limit [Å] | 2.330 | 6.320 | 2.330 |
| Rmerge | 0.081 | 0.032 | 0.761 |
| Rmeas | 0.087 | 0.035 | 0.840 |
| Rpim | 0.032 | 0.013 | 0.349 |
| Total number of observations | 209601 | ||
| Number of reflections | 28397 | 1464 | 1418 |
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 100.0 | 99.7 | 99.4 |
| Redundancy | 7.4 | 7.1 | 5.6 |
| CC(1/2) | 0.999 | 0.785 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | PEG 8000, Mg acetate, MES buffer |
