1CK1
STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ELLIOTT GX-20 |
Temperature [K] | 275 |
Detector technology | AREA DETECTOR |
Collection date | 1993-04 |
Detector | SIEMENS |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 43.700, 43.700, 280.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.600 |
Rwork | 0.162 |
R-free | 0.23300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MIRAS-SOLVED IDENTICAL STRUCTURE IN A DIFFERENT CRYSTAL SETTING |
RMSD bond length | 0.008 |
RMSD bond angle | 25.827 * |
Data reduction software | CCP4 |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.720 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.055 * | 0.112 * |
Number of reflections | 8889 | |
<I/σ(I)> | 10.1 | 5.8 |
Completeness [%] | 91.5 | 76.7 |
Redundancy | 4.6 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | 22 and 37 * | Bohach, G.A., (1992) Proteins, 13, 152. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-10 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 500 (mM) | pH8.5 |