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 | 











