6KIN
Crystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholzii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-07-18 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97893 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 122.033, 133.417, 139.595 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.225 - 2.527 |
R-factor | 0.1784 |
Rwork | 0.176 |
R-free | 0.23370 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4l7z |
RMSD bond length | 0.008 |
RMSD bond angle | 0.926 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.097 | 0.387 |
Rpim | 0.047 | 0.186 |
Number of reflections | 73219 | 3642 |
<I/σ(I)> | 7.3 | |
Completeness [%] | 96.6 | 97.9 |
Redundancy | 4.6 | |
CC(1/2) | 0.987 | 0.905 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289 | The protein sample was mixed with an equal volume of the reservoir solution (16 % (v/v) PEG3350 and 0.2 M sodium chloride), and the mixture was equilibrated against the reservoir solution. |