2E10
Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii, Mutation R51A
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 | 2006-06-04 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.298, 82.654, 72.424 |
Unit cell angles | 90.00, 103.49, 90.00 |
Refinement procedure
Resolution | 29.210 - 1.350 |
R-factor | 0.209 |
Rwork | 0.209 |
R-free | 0.22500 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2dve |
RMSD bond length | 0.005 |
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] | 40.000 | 1.400 |
High resolution limit [Å] | 1.350 | 1.350 |
Rmerge | 0.041 | 0.289 |
Number of reflections | 93074 | |
<I/σ(I)> | 17.2 | 2.3 |
Completeness [%] | 97.0 | 91.6 |
Redundancy | 3.4 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.2 | 295 | PEG 20K, Acetate, NaOH, pH 5.2, microbatch, temperature 295K |