4XFP
Crystal Structure of Highly Active Mutant of Bacillus sp. TB-90 Urate Oxidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-27 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 134.135, 145.195, 71.141 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.818 - 1.660 |
| R-factor | 0.1571 |
| Rwork | 0.156 |
| R-free | 0.18410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wlv |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.030 |
| Data reduction software | SCALEPACK |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1.9-1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.680 |
| High resolution limit [Å] | 1.650 | 4.470 | 1.650 |
| Rmerge | 0.074 | 0.034 | 0.816 |
| Rmeas | 0.080 | 0.037 | 0.887 |
| Rpim | 0.031 | 0.014 | 0.342 |
| Total number of observations | 944905 | ||
| Number of reflections | 157977 | ||
| <I/σ(I)> | 9.9 | ||
| Completeness [%] | 94.3 | 99.1 | 91.6 |
| Redundancy | 6 | 7.1 | 6.1 |
| CC(1/2) | 0.999 | 0.783 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 15% PEG 8000, 0.1M TRIS-HCl, 0.07M K2SO4, |
