4LZW
X-ray structure uridine phosphorylase from Vibrio cholerae in complex with thymidine at 1.29 A resolution
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 | 2012-05-09 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.81 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 91.740, 95.850, 91.830 |
| Unit cell angles | 90.00, 119.96, 90.00 |
Refinement procedure
| Resolution | 19.890 - 1.290 |
| R-factor | 0.1793 |
| Rwork | 0.178 |
| R-free | 0.21050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4g8j |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.324 |
| Data reduction software | MOSFLM |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.650 | 30.000 | 1.340 |
| High resolution limit [Å] | 1.290 | 20.000 | 1.290 |
| Rmerge | 0.113 | 0.150 | 0.842 |
| Number of reflections | 342543 | 57 | 36724 |
| <I/σ(I)> | 9.29 | 6.74 | 2.02 |
| Completeness [%] | 99.2 | 50.4 | 99.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 286 | 0.2 M MgCl2.6H2O, 15%(w/v) polyethylene glycol (PEG) 4000 in 0.1 M Tris HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 286K |
