133L
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 | 57.110, 61.140, 33.130 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.770 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.750 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.770 * |
| Number of reflections | 10122 * |
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 | 5 (M) |
