2HNI
Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3, K111A mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-11-08 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.362, 82.740, 72.945 |
Unit cell angles | 90.00, 103.62, 90.00 |
Refinement procedure
Resolution | 22.720 - 1.900 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.22500 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2djz |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.048 | 0.286 |
Number of reflections | 34116 | |
<I/σ(I)> | 16.8 | 3.4 |
Completeness [%] | 97.7 | 84 |
Redundancy | 3.4 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.2 | 295 | PEG 20000, Acetate, NaOH, pH 5.2, VAPOR DIFFUSION, SITTING DROP, temperature 295K |