2HEF
CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
Experimental procedure
Detector technology | IMAGE PLATE |
Collection date | 1996-09-02 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.750, 60.970, 33.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.16 |
Rwork | 0.160 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.520 |
Data reduction software | PROCESS |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
High resolution limit [Å] | 1.800 | |
Rmerge | 0.033 | 0.085 * |
Total number of observations | 36537 * | |
Number of reflections | 10724 | |
Completeness [%] | 94.0 | 84.6 * |
Redundancy | 3.41 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 * | 10 * |
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) |