1B5W
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 | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 283 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1997-11-27 |
| Detector | WEISSENBERG |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.570, 60.710, 33.520 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.170 |
| R-factor | 0.16 * |
| Rwork | 0.155 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.550 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.250 |
| High resolution limit [Å] | 2.170 | 2.170 |
| Rmerge | 0.060 | 0.094 |
| Total number of observations | 29351 * | |
| Number of reflections | 6404 | |
| <I/σ(I)> | 21.4 | 11.3 |
| Completeness [%] | 97.7 | 89 |
| Redundancy | 4.6 | 4.2 |
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) |
