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)) |
