3UAO
Structure and Catalytic Mechanism of the Vitamin B3 Degradative Enzyme Maleamate Amidohydrolase from Bordetalla bronchiseptica RB50
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OXFORD DIFFRACTION ENHANCE ULTRA |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 2010-08-31 |
Detector | OXFORD RUBY CCD |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 |
Unit cell lengths | 157.560, 157.560, 198.480 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 12.010 - 2.399 |
R-factor | 0.12796 |
Rwork | 0.127 |
R-free | 0.17252 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1NBA MODIFIED TO TARGET SEQUENCE USING PHYRE SERVER |
RMSD bond length | 0.017 |
RMSD bond angle | 1.626 |
Data reduction software | CrysalisPro |
Data scaling software | CrysalisPro |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 12.010 | 2.520 |
High resolution limit [Å] | 2.399 | 2.399 |
Number of reflections | 131825 | |
<I/σ(I)> | 9.78 | |
Completeness [%] | 91.7 | 67.5 |
Redundancy | 2.2 | 1.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 0.2 M ammonium acetate, 0.1 M sodium cacodylate, 30% PEG-8000, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 295K |