1G0K
CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152C
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | OTHER |
Temperature [K] | 300 |
Detector technology | AREA DETECTOR |
Collection date | 1994-10-28 |
Detector | OTHER |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 60.690, 60.690, 96.550 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.850 |
Rwork | 0.155 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.900 |
Data reduction software | SDMS |
Data scaling software | UCSD-system |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.810 |
High resolution limit [Å] | 1.850 * | 1.680 |
Rmerge | 0.048 | 0.211 |
Number of reflections | 20066 | |
<I/σ(I)> | 12.1 | |
Completeness [%] | 87.0 * | 58.4 |
Redundancy | 2.1 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.8 | 277 | Eriksson, A.E., (1993) J. Mol. Biol., 229, 747. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | 0.25 (M) | ||
3 | 1 | reservoir | phosphate | 2.0 (M) | |
4 | 1 | reservoir | beta-mercaptoethanol |