3DTD
Crystal structure of invasion associated protein b from bartonella henselae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 77 |
Detector technology | CCD |
Collection date | 2008-06-30 |
Detector | MAR CCD 165 mm |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 95.707, 139.951, 179.075 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.350 |
R-factor | 0.23591 |
Rwork | 0.235 |
R-free | 0.26524 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.249 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXCD |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.430 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.120 | 0.920 |
Number of reflections | 100682 | |
<I/σ(I)> | 4 | 0.5 |
Completeness [%] | 99.7 | 98.7 |
Redundancy | 6.4 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 294 | 200mM Trimethylamine N-oxide, 100MM TRIS-HCL, PH 8, 20% PEG MME 2000, 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K, pH 8.00 |