1IYD
CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-11-26 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 154.270, 99.020, 138.630 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 * - 2.150 |
Rwork | 0.205 |
R-free | 0.24200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.350 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.960 | 2.220 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.070 * | 0.195 * |
Total number of observations | 324820 * | |
Number of reflections | 58165 | |
Completeness [%] | 99.5 | 96.8 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | 293 | PEG400, HEPES, MgCl2, 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 | 40 (mg/ml) | |
2 | 1 | drop | PEG400 | 42 (%(v/v)) | |
3 | 1 | drop | 200 (mM) | ||
4 | 1 | drop | glutamate | 50 (mM) | |
5 | 1 | drop | sodium HEPES | 100 (mM) | pH7.5 |
6 | 1 | reservoir | PEG400 | 50 (%(v/v)) | |
7 | 1 | reservoir | glutarate | 100 (mM) | |
8 | 1 | reservoir | glutamate | 50 (mM) |