1T4M
STRUCTURE OF A THERMOSTABLE DOUBLE MUTANT OF BACILLUS SUBTILIS LIPASE OBTAINED THROUGH DIRECTED EVOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-04-03 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 |
Unit cell lengths | 76.015, 76.015, 103.093 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.190 - 2.000 |
R-factor | 0.207 |
Rwork | 0.206 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1i6w |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP (CCP4) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 14102 | |
<I/σ(I)> | 19 | 2.4 |
Completeness [%] | 94.0 | 63.2 |
Redundancy | 2.1 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | PEG 3350, ethanolamine, n-octyl-beta-D-glucoside, sodium sulfate., pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 100K |