4MUS
Crystal structure of vancomycin resistance D,D-dipeptidase/D,D-pentapeptidase VanXYc D59S mutant in complex with D-Ala-D-Ala phosphinate analog
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-07-26 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.27696 |
| Spacegroup name | P 1 |
| Unit cell lengths | 44.256, 44.780, 62.407 |
| Unit cell angles | 86.84, 77.29, 64.15 |
Refinement procedure
| Resolution | 37.198 - 1.675 |
| R-factor | 0.1697 |
| Rwork | 0.168 |
| R-free | 0.20710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4f78 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.289 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.670 | 1.870 |
| High resolution limit [Å] | 1.670 | 1.670 |
| Rmerge | 0.086 | 0.396 |
| Number of reflections | 47059 | |
| <I/σ(I)> | 19.6 | 4.9 |
| Completeness [%] | 97.3 | 94.2 |
| Redundancy | 8.1 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 273 | 0.1 M magnesium chloride, 0.05 M MES, 20% PEG 8K, 50 mM PHY D-Ala-D-Ala phosphinate analog, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 273K |
