3AB9
Crystal Structure of lipoylated E. coli H-protein (reduced form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-03-06 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 60.255, 60.255, 68.586 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.650 |
| R-factor | 0.20487 |
| Rwork | 0.204 |
| R-free | 0.21630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hpc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.167 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.670 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.055 | 0.361 |
| Number of reflections | 15779 | |
| <I/σ(I)> | 79.8 | 8.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14.1 | 14.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 288 | 95mM Hepes-Na, 0.19M CaCl2, 26.6% PEG400, 5% Glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
