1DI5
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
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] | 100 |
Detector technology | DIFFRACTOMETER |
Collection date | 1998-10-25 |
Detector | WEISSENBERG |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.420, 61.690, 32.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.165 |
Rwork | 0.165 |
Data reduction software | DENZO |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.042 | 0.088 |
Total number of observations | 27719 * | |
Number of reflections | 5952 | |
Completeness [%] | 97.3 | 84.3 |
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) |