1HN1
E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 153.900, 171.400, 204.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.000 |
Rwork | 0.148 |
R-free | 0.29900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dp0 |
RMSD bond length | 0.015 |
RMSD bond angle | 2.678 |
Data scaling software | SCALEPACK |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.000 | |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.092 | 0.292 |
Number of reflections | 103758 | |
<I/σ(I)> | 7.2 | 2.3 |
Completeness [%] | 95.1 | 98.5 |
Redundancy | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 288 | Juers, D.H., (2000) Protein Sci., 9, 1685., used seeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 10 (%) | |
3 | 1 | reservoir | Bis-Tris | 100 (mM) | |
4 | 1 | reservoir | 200 (mM) | ||
5 | 1 | reservoir | 100 (mM) | ||
6 | 1 | reservoir | dithiothreitol | 10 (mM) |