5MHA
D-2-hydroxyacid dehydrogenases (D2-HDH) from Haloferax mediterranei in complex with a mixture of 2-ketohexanoic acid and 2-hydroxyhexanoic acid, and NADPH (1.57 A resolution)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.540, 76.300, 66.990 |
| Unit cell angles | 90.00, 97.04, 90.00 |
Refinement procedure
| Resolution | 38.150 - 1.570 |
| R-factor | 0.17571 |
| Rwork | 0.174 |
| R-free | 0.21602 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.549 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.150 | 1.610 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Rmerge | 0.039 | 0.397 |
| Number of reflections | 81835 | |
| <I/σ(I)> | 13.6 | 2.2 |
| Completeness [%] | 94.8 | 93.7 |
| Redundancy | 2.1 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 290 | Protein buffer: 20 mM Tris_HCl pH8, 3 mM EDTA and 1 M NaCl Crystallisation conditions: 0.1 M Tris-HCl pH8, 0.5 M Mg acetate and 24 % PEG3350 Ligands: 5 mM NADPH and 50 mM 2-ketohexanoic acid |
