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 |