1YAB
Structure of T. maritima FliN flagellar rotor protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-01-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.979277 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 100.173, 100.173, 87.853 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.900 - 3.400 |
R-factor | 0.22735 |
Rwork | 0.224 |
R-free | 0.28624 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1O6A.pdb |
RMSD bond length | 0.014 |
RMSD bond angle | 1.760 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 87.700 | 3.520 |
High resolution limit [Å] | 3.400 | 3.400 |
Number of reflections | 7246 | |
<I/σ(I)> | 7.3 | 1.8 |
Completeness [%] | 95.9 | 93.4 |
Redundancy | 11 | 11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.9 | 293 | 18% MPD, 100mM MES buffer, pH 5.9, VAPOR DIFFUSION, SITTING DROP, temperature 293K |