4OGM
MBP-fusion protein of PilA1 residues 26-159
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2013-12-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 66.224, 74.710, 97.517 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.264 - 2.234 |
R-factor | 0.1911 |
Rwork | 0.186 |
R-free | 0.24640 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.108 |
Data scaling software | Aimless (0.1.26) |
Phasing software | PHASER (2.5.5) |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.264 | 39.260 | 2.310 |
High resolution limit [Å] | 2.230 | 8.930 | 2.230 |
Rmerge | 0.212 | 0.013 | 0.013 |
Total number of observations | 5347 | 20946 | |
Number of reflections | 23856 | ||
<I/σ(I)> | 13.5 | 59.7 | 1.9 |
Completeness [%] | 98.8 | 98.9 | 87.4 |
Redundancy | 14.1 | 12 | 11.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 25% PEG3350, 0.1 M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |