1B5X
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 173 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1998-04-11 |
| Detector | WEISSENBERG |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.360, 62.620, 32.550 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.152 |
| Rwork | 0.152 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.530 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.071 | 0.155 |
| Total number of observations | 23122 * | |
| Number of reflections | 7913 | |
| <I/σ(I)> | 20.3 | 8.1 |
| Completeness [%] | 95.7 | 96.4 |
| Redundancy | 2.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 | 10 * | Takano, K., (1995) J.Mol.Biol., 254, 62. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | 2.5 (M) | ||
| 3 | 1 | reservoir | acetate | 20 (mM) |
