8SAA
Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes, PLP and phosphate bound (C2 form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-02-14 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9795 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.092, 131.708, 82.624 |
Unit cell angles | 90.00, 104.41, 90.00 |
Refinement procedure
Resolution | 33.480 - 1.450 |
R-factor | 0.1442 |
Rwork | 0.143 |
R-free | 0.16010 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.901 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.21rc1_4906: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 80.030 | 1.490 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.072 | 1.308 |
Rmeas | 0.078 | 1.417 |
Rpim | 0.029 | 0.539 |
Total number of observations | 1088962 | 77576 |
Number of reflections | 156782 | 11427 |
<I/σ(I)> | 12.3 | 1.5 |
Completeness [%] | 98.7 | |
Redundancy | 6.9 | 6.8 |
CC(1/2) | 0.999 | 0.724 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | Morpueus C9: 20%(v/v) PEG 500 MME, 10%(w/v) PEG 20000, 100 mM Tris/BICINE, pH 8.5, 30 mM NaNO3, 30 mM Na2HPO4 and 30 mM (NH4)2SO4, 2mM PLP and 2mM Arginine added to the protein prior to crystallization, KlaeA.00906.a.B1.PW39169 at 41.1 mg/mL. Plate: 13220, well C9 drop 3, Puck: PSL-0505, Cryo: Direct |