5AWV
Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin
Replaces: 4K3TReplaces: 2WDXExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.791, 150.778, 124.853 |
| Unit cell angles | 90.00, 98.40, 90.00 |
Refinement procedure
| Resolution | 29.400 - 1.930 |
| R-factor | 0.15842 |
| Rwork | 0.156 |
| R-free | 0.20464 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wdw |
| RMSD bond length | 0.022 |
| RMSD bond angle | 2.162 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.510 | 1.960 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.091 | 0.573 |
| Number of reflections | 163843 | |
| <I/σ(I)> | 14.97 | 2.87 |
| Completeness [%] | 97.8 | 97.1 |
| Redundancy | 4.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 17% PEG 3350, 0.2M diammonium hydrogen citrate, pH 5.0 |
