2MEG
CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-18B |
Synchrotron site | Photon Factory |
Beamline | BL-18B |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1996-12-12 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.100, 61.060, 33.760 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.151 |
Rwork | 0.151 |
Structure solution method | ISOMORPHOUS METHOD |
Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
RMSD bond length | 0.008 |
RMSD bond angle | 23.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.830 | |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.052 | 0.180 |
Total number of observations | 42094 * | |
Number of reflections | 10582 * | |
<I/σ(I)> | 8.8 | |
Completeness [%] | 92.2 | 80.9 |
Redundancy | 2.5 |
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) |