1WLG
Crystal structure of FlgE31, a major fragment of the hook protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2001-06-27 |
| Detector | ADSC |
| Wavelength(s) | 0.92 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 128.714, 49.034, 96.904 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.19285 |
| Rwork | 0.190 |
| R-free | 0.24153 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.431 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Outer shell | |
| Low resolution limit [Å] | 1.846 |
| High resolution limit [Å] | 1.800 |
| Completeness [%] | 97 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 289 | PEG 2000, copper acetate, cacodylate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
