5TQI
Crystal structure of a pyridoxal kinase from Burkholderia multivorans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-04-13 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 82.970, 42.490, 90.510 |
Unit cell angles | 90.00, 115.56, 90.00 |
Refinement procedure
Resolution | 40.826 - 1.500 |
R-factor | 0.1386 |
Rwork | 0.138 |
R-free | 0.17780 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.796 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 44.900 | 1.540 | |
High resolution limit [Å] | 1.500 | 6.710 | 1.500 |
Rmerge | 0.076 | 0.049 | 0.492 |
Number of reflections | 91157 | ||
<I/σ(I)> | 11.27 | 24.72 | 2.82 |
Completeness [%] | 99.3 | 94.5 | 98.8 |
Redundancy | 3.73 | ||
CC(1/2) | 0.996 | 0.995 | 0.807 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 290 | RigakuReagents JCSG+ screen, B3: 20% PEG 6000, 100 mM BICINE; BumuA.00129.a.B1.PS37843 at 18.12 mg/ml; cryo: 20% EG, 2 steps; tray 270818b3, puck fsu3-5 |