1G19
STRUCTURE OF RECA PROTEIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-07-15 |
Detector | MARRESEARCH |
Spacegroup name | P 61 |
Unit cell lengths | 108.072, 108.072, 72.783 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 3.000 |
R-factor | 0.218 * |
Rwork | 0.217 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | ESCHERICHIA COLI RECA (2REB) |
RMSD bond length | 0.017 * |
RMSD bond angle | 2.290 * |
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 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.107 | 0.537 |
Number of reflections | 9654 | |
<I/σ(I)> | 17.2 | 4.9 |
Completeness [%] | 98.4 | 98 |
Redundancy | 6.2 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | Phosphate-Citrate, PEG 4000, AlF4, ADP, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | phosphate-citrate | 100 (mM) | |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | PEG4000 | 6 (%) | |
5 | 1 | reservoir | PEG4000 | 20 (%) | |
6 | 1 | reservoir | phosphate-citrate | 100 (mM) |