1E6P
Chitinase B from Serratia marcescens inactive mutant E144Q
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-03-27 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.134, 104.138, 186.654 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.810 - 1.700 |
R-factor | 0.182 |
Rwork | 0.182 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e15 |
RMSD bond length | 0.011 |
RMSD bond angle | 23.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.063 | 0.400 |
Total number of observations | 465926 * | |
Number of reflections | 118061 | 10746 * |
<I/σ(I)> | 13.6 | 2.3 |
Completeness [%] | 97.7 | 90.2 |
Redundancy | 3.9 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.6 * | Van Aalten, D.M.F., (2000) Proc. Natl. Acad. Sci. U.S.A., 97, 5842. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | citrate | 50 (mM) | |
3 | 1 | reservoir | 0.5 (M) | ||
4 | 1 | reservoir | ammonium sulfate | 0.25 (M) |