1I1K
CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200H |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1996-12-11 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 100.930, 156.060, 141.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.100 |
R-factor | 0.189 * |
Rwork | 0.189 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.200 |
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] | 30.000 | |
High resolution limit [Å] | 2.100 | 2.100 * |
Rmerge | 0.049 * | 0.193 * |
Total number of observations | 197817 * | |
Number of reflections | 62258 * | |
Completeness [%] | 95.3 * | 88.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 20 * | PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 35 (mg/ml) | |
2 | 1 | drop | HEPES | 0.1 (M) | |
3 | 1 | drop | PLP | 0.010 (mM) | |
4 | 1 | drop | sodium azide | 1 (mM) | |
5 | 1 | reservoir | PEG400 | 28 (%(w/v)) | |
6 | 1 | reservoir | 0.1 (M) |