2SAK
STAPHYLOKINASE (SAKSTAR VARIANT)
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Collection date | 1995-06 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 60.600, 43.730, 54.270 |
Unit cell angles | 90.00, 115.63, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.800 |
R-factor | 0.181 |
Rwork | 0.181 |
R-free | 0.23700 |
Structure solution method | MIR |
RMSD bond length | 0.010 |
RMSD bond angle | 26.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.820 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.034 * | |
Total number of observations | 76483 * | |
Number of reflections | 11949 | |
<I/σ(I)> | 25 | 8.5 |
Completeness [%] | 95.8 | 100 |
Redundancy | 6.4 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | Rabijins, A., (1997) Protein.Struct.Funct.Genet., 27, 160. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 0.1 (M) | ||
2 | 1 | drop | Tris-HCl | 0.05 (M) | |
3 | 1 | drop | PEG4000 | 17.5 (%) | |
4 | 1 | drop | protein | 17.5 (mg/ml) | |
5 | 1 | drop | HEPES | 25 (mM) | |
6 | 1 | reservoir | 0.2 (M) | ||
7 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
8 | 1 | reservoir | PEG4000 | 35 (%) |