1P3N
CORE REDESIGN BACK-REVERTANT I103V/CORE10
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-08-24 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 59.999, 59.999, 95.941 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 23.973 - 1.550 |
R-factor | 0.189 |
Rwork | 0.186 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1l63 |
RMSD bond length | 0.015 * |
RMSD bond angle | 2.300 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.973 | 1.600 |
High resolution limit [Å] | 1.550 * | 1.550 |
Rmerge | 0.060 * | 0.286 |
Number of reflections | 28432 | |
<I/σ(I)> | 6.6 | 2.4 |
Completeness [%] | 96.7 | 97 |
Redundancy | 3.7 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.7 | 277 | Eriksson, A.E., (1993) J.Mol.Biol., 229, 747. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | 0.25 (M) | ||
3 | 1 | reservoir | phosphate | 2.0 (M) | |
4 | 1 | reservoir | beta-mercaptoethanol |