2E1H
Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3, K111G mutation
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 | IMAGE PLATE |
| Collection date | 2006-06-04 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.305, 82.848, 73.161 |
| Unit cell angles | 90.00, 104.69, 90.00 |
Refinement procedure
| Resolution | 29.860 - 1.400 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.23000 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 2deq |
| 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] | 40.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.044 | 0.390 |
| Number of reflections | 78962 | |
| <I/σ(I)> | 11.4 | 2.3 |
| Completeness [%] | 91.1 | 81 |
| Redundancy | 3.1 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.2 | 295 | PEG 20K, Acetate, NaOH, pH 5.2, microbatch, temperature 295K |
