1FHU
CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-12-07 |
Detector | SBC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.100, 70.000, 80.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.650 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.26500 |
RMSD bond length | 0.014 |
RMSD bond angle | 16.110 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.069 | 0.294 |
Number of reflections | 36924 * | |
<I/σ(I)> | 14.1 | |
Completeness [%] | 99.0 | 98.4 |
Redundancy | 11.4 | 11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 6.75 | 296 | 27% ME-PEG 5000, 267 mM NaCl, 50 mM Mes, 15-20 mg/ml protein, pH 6.75, micro batch, temperature 23K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15-20 (mg/ml) | |
2 | 1 | 1 | mPEG5000 | 27 (%) | |
3 | 1 | 1 | 267 (mM) | ||
4 | 1 | 1 | MES | 50 (mM) |