2E65
Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3, Mutation D104A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-11-25 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.365, 82.596, 72.579 |
Unit cell angles | 90.00, 102.96, 90.00 |
Refinement procedure
Resolution | 36.620 - 1.650 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.22400 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2dxt |
RMSD bond length | 0.007 |
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] | 41.300 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.065 | 0.282 |
Number of reflections | 50943 | |
<I/σ(I)> | 12.5 | 2.1 |
Completeness [%] | 96.8 | 90.7 |
Redundancy | 3.2 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.2 | 295 | PEG20K, Acetate, NaOH, pH 5.2, microbatch, temperature 295K |