1N1A
Crystal Structure of the N-terminal domain of human FKBP52
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-01-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 27.805, 58.362, 70.904 |
Unit cell angles | 90.00, 98.31, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.400 |
R-factor | 0.219 |
Rwork | 0.204 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fkj |
RMSD bond length | 0.018 * |
RMSD bond angle | 2.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.095 | 0.294 |
Total number of observations | 26262 * | |
Number of reflections | 8929 * | 889 * |
<I/σ(I)> | 17.3 | 9.3 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 10.8 | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | Tris-HCl, Ammonium Sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | sodium cacodylate | 10 (mM) | |
2 | 1 | drop | protein | 20-30 (mg/ml) | |
3 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |