1DI4
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 288 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-05-20 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.800, 59.270, 38.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.165 |
| Rwork | 0.165 |
| Data reduction software | PROCESS |
| Data scaling software | PROCESS |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 4.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.081 | 0.201 |
| Total number of observations | 20055 * | |
| Number of reflections | 7155 | |
| Completeness [%] | 94.1 | 87.8 |
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) |
