3LV0
Crystal structure of extragenic suppressor protein suhB from Bartonella henselae, native
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 | 2010-01-13 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 82.060, 138.600, 67.240 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.850 |
R-factor | 0.19257 |
Rwork | 0.191 |
R-free | 0.21816 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3luz |
RMSD bond length | 0.015 |
RMSD bond angle | 1.434 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.610 | 1.900 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.061 | 0.552 |
Number of reflections | 66080 | |
<I/σ(I)> | 19.58 | 3.5 |
Completeness [%] | 99.8 | 99.2 |
Redundancy | 7.9 | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 24 mg/mL protein against 0.2M MgCl2, 0.1 M Tris pH 8.5, 30% PEG 400, crystal tracking ID 205526c1, VAPOR DIFFUSION, SITTING DROP, temperature 289K |