1UBC
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 | 2000-11-05 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 |
Unit cell lengths | 103.441, 103.441, 71.765 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 * - 3.800 |
R-factor | 0.242 |
Rwork | 0.242 |
R-free | 0.30500 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g19 |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.940 |
High resolution limit [Å] | 3.800 | 3.800 |
Rmerge | 0.152 * | 0.479 * |
Number of reflections | 4340 | 434 * |
<I/σ(I)> | 2 | |
Completeness [%] | 98.5 | 99.3 |
Redundancy | 4.6 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PEG 4000, CIT-PHOS, NACL, DTT, 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 | 6 (mg/ml) | |
2 | 1 | drop | citrate-phosphate | 100 (mM) | pH7.5 |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | dithiothreitol | 0.2 (mM) | |
5 | 1 | drop | ammonium acetate | 0.1 (M) | |
6 | 1 | drop | PEG4000 | 6 (%) | |
7 | 1 | reservoir | PEG4000 | 25 (%) |