1GT9
High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.860, 78.250, 73.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.520 - 1.380 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.20800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ga1 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.630 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.520 | 1.410 |
High resolution limit [Å] | 1.380 | 1.380 |
Rmerge | 0.064 * | 0.232 |
Total number of observations | 603967 * | |
Number of reflections | 120406 * | |
Completeness [%] | 95.5 | 79 |
Redundancy | 4.8 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 5 * | 20 * | 100 MM SODIUM ACETATE PH 4.5, 400 MM AMMONIUM SULPHATE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 9 (mg/ml) | |
2 | 1 | drop | 25 (mM) | ||
3 | 1 | drop | sodium acetate | 50 (mM) | pH5. |
4 | 1 | reservoir | ammonium sulfate | 1.2 (M) | |
5 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.2 |