1BG5
CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 1996-06 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 92.170, 92.170, 57.570 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.600 |
R-factor | 0.193 |
Rwork | 0.193 |
R-free | 0.35900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gta |
RMSD bond length | 0.009 |
RMSD bond angle | 29.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 8.000 | 2.710 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.058 | 0.050 |
Number of reflections | 7078 | |
<I/σ(I)> | 10.7 | 3.1 |
Completeness [%] | 86.0 | 81 |
Redundancy | 2.6 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.8 | i * | pH 8.8 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 50 (mM) | |
2 | 1 | drop | 150 (mM) | ||
3 | 1 | drop | beta-mercaptoethanol | 2 (mM) | |
4 | 1 | reservoir | PEG4000 | 30 (%) | |
5 | 1 | reservoir | bis-tris-propane | 100 (mM) | |
6 | 1 | reservoir | 150 (mM) | ||
7 | 1 | reservoir | beta-mercaptoethanol | 0.04 (M) |