2HEB
CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6B |
Synchrotron site | Photon Factory |
Beamline | BL-6B |
Detector technology | IMAGE PLATE |
Collection date | 1996-12-07 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.800, 61.220, 33.760 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.124 |
Rwork | 0.124 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.520 |
Data reduction software | DENZO |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
High resolution limit [Å] | 2.000 * | |
Rmerge | 0.071 | 0.185 * |
Total number of observations | 21591 * | |
Number of reflections | 5702 | |
Completeness [%] | 67.7 | 56.2 * |
Redundancy | 3.87 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 * | 10 * | Takano, K., (1997) Biochemistry, 36, 688. * |
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) |