8SA9
Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes, PLP-Oxamate Adduct (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 | 87.313, 131.511, 82.585 |
Unit cell angles | 90.00, 103.81, 90.00 |
Refinement procedure
Resolution | 26.860 - 1.100 |
R-factor | 0.1252 |
Rwork | 0.125 |
R-free | 0.13700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.023 |
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] | 80.200 | 1.130 |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.056 | 1.056 |
Rmeas | 0.061 | 1.229 |
Rpim | 0.023 | 0.617 |
Total number of observations | 2207969 | 59166 |
Number of reflections | 345136 | 15798 |
<I/σ(I)> | 12.4 | 1.1 |
Completeness [%] | 94.7 | |
Redundancy | 6.4 | 3.7 |
CC(1/2) | 0.999 | 0.574 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | Morpueus G9: 20%(v/v) PEG 500 MME, 10%(w/v) PEG 20000, 100 mM Tris/BICINE, pH 8.5, 20 mM Sodium formate, 20 mM Ammonium acetate, 20 mM Sodium citrate tribasic, 20 mM Potassium sodium tartrate and 20 mM Sodium oxamate, 2mM PLP added to the protein prior to crystallization, KlaeA.00906.a.B1.PW39169 at 41.1 mg/mL. Plate: 13220, well G9 drop 3, Puck: PSL-0416, Cryo: Direct |