1B5U
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-18B |
Synchrotron site | Photon Factory |
Beamline | BL-18B |
Temperature [K] | 283 |
Detector technology | DIFFRACTOMETER |
Collection date | 1996-10-31 |
Detector | WEISSENBERG |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.960, 60.980, 33.780 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.156 |
Rwork | 0.156 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
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] | 40.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.036 | 0.113 |
Total number of observations | 47257 * | |
Number of reflections | 10868 | |
<I/σ(I)> | 36.8 | 13.2 |
Completeness [%] | 95.2 | 85.7 |
Redundancy | 4.3 | 4 |
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) |