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) |