2WHY
Crystal structure of the triscatecholate siderophore binding protein FeuA from Bacillus subtilis complexed with Ferri-Bacillibactin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-24 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.530, 63.140, 55.530 |
| Unit cell angles | 90.00, 110.44, 90.00 |
Refinement procedure
| Resolution | 19.510 - 1.700 |
| R-factor | 0.16042 |
| Rwork | 0.157 |
| R-free | 0.19120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2phz |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.159 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.760 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.040 | 0.520 |
| Number of reflections | 28022 | |
| <I/σ(I)> | 20.1 | 3.4 |
| Completeness [%] | 99.2 | 99.5 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.2 | PROTEIN WAS CRYSTALLIZED FROM 30% (V/V) PEG 600, 100 MM PHOSPHATE-CITRATE, PH 5.2; THEN SOAKED IN MOTHER LIQUOR CONTAINING 30% (V/V) GLYCEROL FOR CRYO PROTECTION. |
