4MCH
Crystal structure of uridine phosphorylase from vibrio fischeri es114 complexed with 6-hydroxy-1-naphthoic acid, NYSGRC Target 029520.
Experimental procedure
| Experimental method | SAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-08-13 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9791 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 163.975, 163.975, 58.355 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.160 - 1.730 |
| R-factor | 0.1741 |
| Rwork | 0.173 |
| R-free | 0.19620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lnh |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.196 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA (3.2.5) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.753 | 19.753 | 1.820 |
| High resolution limit [Å] | 1.730 | 5.470 | 1.730 |
| Rmerge | 0.103 | 0.015 | 0.015 |
| Total number of observations | 6522 | 32166 | |
| Number of reflections | 31147 | ||
| <I/σ(I)> | 7.9 | 18 | 0.5 |
| Completeness [%] | 99.6 | 88.7 | 100 |
| Redundancy | 7.2 | 7.1 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.2 M AMMONIUM SULFATE, 0.1 M HEPES:NAOH, PH 8.5, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
