1JTM
Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet has Weak Intrinsic Folding Propensity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 170 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-07-21 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.970, 60.970, 97.345 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 17.000 - 1.900 |
| R-factor | 0.214 * |
| Rwork | 0.214 |
| R-free | 0.26500 |
| Starting model (for MR) | PDB ID 2LZM |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.400 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.000 | 2.010 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.068 * | |
| Number of reflections | 19736 | |
| <I/σ(I)> | 3.9 | 2.6 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 298 | used microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-glycine | 50 (mM) | pH7.5 |
| 2 | 1 | drop | 100 (mM) | ||
| 3 | 1 | drop | protein | 20 (mg/ml) | |
| 4 | 1 | reservoir | PEG8000 | 20 (%(w/v)) | |
| 5 | 1 | reservoir | isopropanol | 10 (%(v/v)) | |
| 6 | 1 | reservoir | phosphate | 50 (mM) | pH7.0 |
