4XY3
Structure of ESX-1 secreted protein EspB
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 72.110, 146.490, 94.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.110 - 3.040 |
| R-factor | 0.2223 |
| Rwork | 0.220 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xxn |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.220 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.110 | 3.200 | |
| High resolution limit [Å] | 3.040 | 13.600 | 3.040 |
| Rmerge | 0.135 | 0.056 | 0.917 |
| Rmeas | 0.151 | 0.062 | 1.170 |
| Total number of observations | 47924 | ||
| Number of reflections | 9487 | 114 | 686 |
| <I/σ(I)> | 8.99 | 19.98 | 1.73 |
| Completeness [%] | 95.7 | 85.1 | 97.5 |
| Redundancy | 5.05 | 5.05 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10.8 | 298 | 0.1M CAPSO, PH 10.8, 0.2M sodium chloride, 1.5M ammonium sulfate |
