3EUF
Crystal structure of BAU-bound human uridine phosphorylase 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.197, 74.442, 262.707 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.20481 |
| Rwork | 0.202 |
| R-free | 0.25147 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1u1c |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.721 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.119 | 0.441 |
| Number of reflections | 103213 | 10192 |
| <I/σ(I)> | 16.1 | 2 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 10.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 17% PEG 3350, 300mM KCl, 30mM MgCl2, 100mM Bis-Tris Buffer, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
