1CUO
CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1997-12-20 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 32.960, 33.670, 47.340 |
Unit cell angles | 90.00, 101.35, 90.00 |
Refinement procedure
Resolution | 19.700 - 1.600 |
R-factor | 0.184 |
Rwork | 0.175 |
R-free | 0.24200 |
RMSD bond length | 0.016 * |
RMSD bond angle | 2.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.700 | 1.630 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.053 | 0.192 |
Number of reflections | 12059 | |
<I/σ(I)> | 6.8 | |
Completeness [%] | 88.2 | 0.739 |
Redundancy | 2.8 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | Inoue, T., (1999) Acta Crystallogr., Sect.D, 55, 307. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | drop | cacodylate | 100 (mM) | |
3 | 1 | drop | PEG4000 | 12.5 (%(w/v)) | |
4 | 1 | reservoir | cacodylate | 100 (mM) | |
5 | 1 | reservoir | PEG4000 | 25 (%(w/v)) |