134L
ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.620, 60.940, 30.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.770 |
R-factor | 0.183 |
Rwork | 0.183 |
RMSD bond length | 0.013 |
RMSD bond angle | 2.780 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.770 * |
Rmerge | 0.083 * |
Total number of observations | 34053 * |
Number of reflections | 9105 * |
Completeness [%] | 80.5 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | used seeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | ammonium nitrate | 7 (M) |