1LGU
T4 Lysozyme Mutant L99A/M102Q
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 2002-03-18 |
Detector | SDMS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 60.800, 60.800, 97.000 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 1.900 |
R-factor | 0.184 * |
Rwork | 0.184 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | wild type T4 lysozyme |
RMSD bond length | 0.016 |
RMSD bond angle | 2.900 |
Data reduction software | SDMS |
Data scaling software | SDMS |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.077 | 0.167 * |
Number of reflections | 15427 | 2393 * |
<I/σ(I)> | 9.7 | 2.4 |
Completeness [%] | 88.0 | 72 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.1 * | 4 * | Lipscomb, L.A., (1998) Protein Sci., 7, 765. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | sodium phosphate | 0.1 (M) | |
2 | 1 | drop | 0.55 (M) | ||
3 | 1 | drop | 0.02 (%) | ||
4 | 1 | reservoir | oxidized beta-mercaptoethanol | 50 (mM) | |
5 | 1 | reservoir | reduced beta-mercaptoethanol | 50 (mM) | |
6 | 1 | reservoir | sodium/potassium phosphate | 1.8-2.0 (M) |