1EP8
CRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTII
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1998-06-04 |
Detector | MACSCIENCE |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 49.692, 49.692, 145.551 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.196 * |
Rwork | 0.196 |
R-free | 0.22000 |
RMSD bond length | 0.018 |
RMSD bond angle | 24.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.047 | 0.170 |
Total number of observations | 53351 * | |
Number of reflections | 10823 | |
<I/σ(I)> | 26.8 | |
Completeness [%] | 96.4 | 91.6 |
Redundancy | 5 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 8000, PEG 10000, Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 18 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 10 (%(w/v)) | |
3 | 1 | reservoir | PEG10000 | 10 (%(w/v)) | |
4 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH6.5 |