1DI3
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 | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.280, 62.960, 32.460 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| Phasing software | X-PLOR |
| 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 | 0.045 | 0.089 |
| Total number of observations | 26966 * | |
| Number of reflections | 10060 | |
| Completeness [%] | 90.8 | 90 |
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) |
