4WY2
Crystal structure of universal stress protein E from Proteus mirabilis in complex with UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-glucosamine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-07-24 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 107.877, 107.877, 74.923 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.1736 |
| Rwork | 0.172 |
| R-free | 0.20180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3olq |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.453 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.080 | 0.040 | 0.892 |
| Rmeas | 0.087 | 0.043 | 0.976 |
| Rpim | 0.033 | 0.016 | 0.389 |
| Total number of observations | 274114 | ||
| Number of reflections | 41254 | ||
| <I/σ(I)> | 9.5 | 1.9 | |
| Completeness [%] | 99.6 | 98.9 | 98.7 |
| Redundancy | 6.6 | 6.5 | 6.1 |
| CC(1/2) | 0.999 | 0.750 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 289 | 0.2 ul of 12 mg/ml protein in 10mM HEPES, 500mM NaCl pH 7.5 were mixed with 0.2 ul of the Quiagen Cryos Suite condition #50 (1.36 M Ammonium Sulfate, 0.085 M MES pH 6.5, 8.5% Dioxane, 15% Glycerol) and equilibrated against the mother liquor in 96 Well 2 drop Crystallization Plate (MRC) |
