1A3G
BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Collection date | 1996-04 |
Detector | RIGAKU |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 135.100, 144.000, 102.900 |
Unit cell angles | 90.00, 136.10, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.500 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.25800 |
Structure solution method | ISOMORPHOUS REPLACEMENT |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.500 |
Rmerge | 0.059 |
Number of reflections | 39622 |
Completeness [%] | 83.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 28% PEG 400, 200MM MGCL2, 100MM HEPES, PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | HEPES | 100 (mM) | |
2 | 1 | reservoir | 200 (mM) | ||
3 | 1 | reservoir | PEG400 | 28 (%(w/v)) |