1BQA
ASPARTATE AMINOTRANSFERASE P195A MUTANT
Experimental procedure
Source type | ROTATING ANODE |
Source details | ELLIOTT |
Temperature [K] | 290 |
Detector technology | IMAGE PLATE |
Collection date | 1996-07 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 88.860, 79.850, 89.520 |
Unit cell angles | 90.00, 119.69, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.199 |
Rwork | 0.195 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ahe |
RMSD bond length | 0.010 |
RMSD bond angle | 24.450 * |
Data reduction software | XDS |
Data scaling software | Agrovata |
Phasing software | AMoRE |
Refinement software | TNT (5D) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.058 | 0.270 |
Number of reflections | 59668 | |
<I/σ(I)> | 10.5 | 3.1 |
Completeness [%] | 92.2 | 89.6 |
Redundancy | 2.6 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | pH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 10 (mM) | |
3 | 1 | drop | PLP | 0.010 (mM) | |
4 | 1 | drop | K2-EDTA | 2 (mM) | |
5 | 1 | drop | dithiothreitol | 0.5 (mM) | |
6 | 1 | reservoir | ammonium sulfate | 1.9-2.1 (M) | |
7 | 1 | reservoir | 2-mercaptoethanol | 0.2 (M) | |
8 | 1 | reservoir | PEG400 | 2 (%) |