6JNK
Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (NADP-bound form)
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 | PIXEL |
| Collection date | 2018-08-04 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.745, 97.526, 104.762 |
| Unit cell angles | 90.00, 104.15, 90.00 |
Refinement procedure
| Resolution | 46.636 - 2.200 |
| R-factor | 0.2117 |
| Rwork | 0.209 |
| R-free | 0.26760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmeas | 0.155 | 1.015 |
| Number of reflections | 68572 | 22054 |
| <I/σ(I)> | 6.26 | |
| Completeness [%] | 99.1 | 97.8 |
| Redundancy | 3.53 | 3.62 |
| CC(1/2) | 0.992 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 25% PEG 3350, 0.1 M Tris-HCl pH 8.5, 0.2 M NaCl |






