1L46
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Experimental procedure
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.000, 61.000, 96.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 1.700 |
R-factor | 0.157 |
RMSD bond length | 0.020 |
RMSD bond angle | 0.017 * |
Refinement software | TNT |
Data quality characteristics
Overall | |
Rmerge | 0.056 * |
Total number of observations | 15933 * |
Number of reflections | 14771 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | taken from Remington, S.J. et al (1978). J. Mol. Biol., 81-98. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 1 | 0.55 (M) | ||
3 | 1 | 1 | mercaptoethanol | 14 (mM) | |
4 | 1 | 1 | 1 (mM) | ||
5 | 1 | 1 | sodium phospahte | 0.01 (M) | |
6 | 1 | 1 | 2.2 (M) | ||
7 | 1 | 1 | 1.8 (M) |