1R17
Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (adhesin-ligand complex)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2001-09-01 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 89.018, 89.483, 98.044 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 1.860 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.22100 |
Structure solution method | MIR |
RMSD bond length | 0.006 |
RMSD bond angle | 1.270 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.930 |
High resolution limit [Å] | 1.860 | 1.860 |
Rmerge | 0.061 * | |
Total number of observations | 549956 * | |
Number of reflections | 63746 | |
<I/σ(I)> | 31.09 | 5.2 |
Completeness [%] | 95.7 * | 92.7 |
Redundancy | 8.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | PEG 2000 MME, NaCl, MES, Pipes, Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG2000 MME | 50 (%) | |
2 | 1 | reservoir | 0.2 (M) |