6LU2
Crystal structure of a substrate binding protein from Microbacterium hydrocarbonoxydans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-10-27 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9785 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.263, 78.443, 123.368 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.551 - 1.750 |
Rwork | 0.194 |
R-free | 0.20640 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.465 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXD |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.780 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.092 | 1.100 |
Number of reflections | 48691 | 2301 |
<I/σ(I)> | 50.6 | 2.8 |
Completeness [%] | 99.3 | 95.7 |
Redundancy | 13.2 | 11.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2 M sodium acetate 0.1 M sodium cacodylate, pH 7.5 30% (w/v) PEG8000 |