1EA0
Alpha subunit of A. brasilense glutamate synthase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-11-15 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 233.612, 233.612, 305.089 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.25618 |
Rwork | 0.256 |
R-free | 0.28712 |
Structure solution method | MAD |
RMSD bond length | 0.024 |
RMSD bond angle | 0.027 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.100 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.092 | 0.456 |
Total number of observations | 758585 * | |
Number of reflections | 184182 | |
<I/σ(I)> | 6.4 | 1.2 |
Completeness [%] | 98.6 | 94.1 |
Redundancy | 4.1 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 * | 20 * | pH 5.60 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 17 (mg/ml) | |
10 | 1 | reservoir | PEG3350 | 15 (%(w/v)) | |
11 | 1 | reservoir | sodium citrate | 100 (mM) | |
2 | 1 | drop | EDTA | 1 (mM) | |
3 | 1 | drop | glycerol | 10 (%(v/v)) | |
4 | 1 | drop | MetS | 2 (mM) | |
5 | 1 | drop | 2-oxoglutarate | 2 (mM) | |
6 | 1 | drop | AADP | 2 (mM) | |
7 | 1 | drop | dithiothreitol | 5 (mM) | |
8 | 1 | drop | HEPES | 25 (mM) | |
9 | 1 | reservoir | tert-butanol | 20 (%(v/v)) |