1DYG
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.800, 60.800, 95.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.100 |
| R-factor | 0.17 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.900 |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.100 * |
| Rmerge | 0.053 * |
| Number of reflections | 11588 * |
| Completeness [%] | 83.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 6.7 * | 4 * | referred to 'Remington, S. J.', (1978) J. Mol. Biol., 118, 81-98 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 20 (mg/ml) | |
| 2 | 1 | 1 | 0.55 (M) | ||
| 3 | 1 | 1 | mercaptoethanol | 14 (mM) | |
| 4 | 1 | 1 | 1 (mM) | ||
| 5 | 1 | 1 | sodium phosphate | 0.01 (M) | |
| 6 | 1 | 1 | 2.2 (M) | one slowly adds 0.8-1.1 portions | |
| 7 | 1 | 1 | 1.8 (M) | one slowly adds 0.8-1.1 portions |
