1DQU
CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02-27 |
Detector | MARRESEARCH |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 91.930, 91.930, 152.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.800 |
R-factor | 0.276 |
Rwork | 0.273 |
R-free | 0.37600 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.500 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | MLPHARE |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.050 | 0.439 |
Total number of observations | 62390 * | |
Number of reflections | 21252 | |
<I/σ(I)> | 13.2 | |
Completeness [%] | 91.5 | 71.9 |
Redundancy | 2.9 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 290 | Langridge, S.J., (1997) Acta Crystallogr., Sect.D, 53, 488. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | PEG2000 | 1-20 (%(w/v)) | |
3 | 1 | drop | sodium HEPES | 0.1 (M) |