2V15
Terbium binding in Streptococcus suis Dpr protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-19 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 104.485, 137.715, 142.438 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.980 - 2.100 |
R-factor | 0.19 |
Rwork | 0.188 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1umn |
RMSD bond length | 0.014 |
RMSD bond angle | 1.412 |
Data reduction software | HKL |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.000 | |
High resolution limit [Å] | 2.000 | 2.100 |
Rmerge | 0.080 | |
Number of reflections | 115331 | |
<I/σ(I)> | 13.9 | |
Completeness [%] | 95.6 | |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 289 | 2UL AND 2UL VOLUME DROP, 30 % PEG 400, 0.2 M CACL2, 0.1 M HEPES-NAOH, PH 7.4, HANGING DROP,16C |