5EFO
X-ray structure uridine phosphorylase from Vibrio cholerae in complex with cytidine and cytosine at 1.63A.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-05-15 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97989 |
| Spacegroup name | P 1 |
| Unit cell lengths | 59.949, 76.336, 89.694 |
| Unit cell angles | 67.54, 73.74, 84.92 |
Refinement procedure
| Resolution | 19.970 - 1.630 |
| R-factor | 0.1652 |
| Rwork | 0.163 |
| R-free | 0.20730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lwz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.191 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.157 | 45.157 | 1.720 |
| High resolution limit [Å] | 1.630 | 5.150 | 1.630 |
| Rmerge | 0.080 | 0.034 | 0.428 |
| Rmeas | 0.096 | ||
| Rpim | 0.053 | 0.022 | 0.281 |
| Total number of observations | 533373 | 17493 | 68525 |
| Number of reflections | 164109 | ||
| <I/σ(I)> | 10.5 | 26.2 | 2.5 |
| Completeness [%] | 93.2 | 94.9 | 84.2 |
| Redundancy | 3.3 | 3.3 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | PEG4000, 0.1M TRIS-HCl, 0.2M MgCl2x6H2O |
