1Q0O
CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM BREVIBACTERIUM FUSCUM (FULL LENGTH PROTEIN)
Replaces: 1F1YExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 291 |
Detector technology | AREA DETECTOR |
Collection date | 1999-01-01 |
Detector | SIEMENS HI-STAR |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 118.900, 118.900, 110.300 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
Rwork | 0.161 |
R-free | 0.20800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.760 |
Data reduction software | X-GEN |
Data scaling software | X-GEN |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.370 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.089 | 0.323 |
Number of reflections | 36551 | |
<I/σ(I)> | 6.7 | 1 |
Completeness [%] | 89.0 | 42.3 |
Redundancy | 4.8 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch | 7.5 | 291 | 1.5 M ammonium sulfate, 100 mM Mops, pH 7.5, Batch, temperature 291K |