8SA8

Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes, Covalently bound and free PLP (I2 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	I 1 2 1
Unit cell lengths	87.887, 131.544, 165.363
Unit cell angles	90.00, 104.48, 90.00

Refinement procedure

Resolution	21.220 - 1.300
R-factor	0.1321
Rwork	0.131
R-free	0.15250
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.040
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]	101.640	1.330
High resolution limit [Å]	1.300	1.300
Rmerge	0.081	1.668
Rmeas	0.087	1.792
Rpim	0.032	0.653
Total number of observations	3067480	227574
Number of reflections	425218	30496
<I/σ(I)>	11.4	1.2
Completeness [%]	95.8
Redundancy	7.2	7.5
CC(1/2)	0.998	0.607

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	Morpueus A10: 20%(v/v) Ethylene glycol, 10%(w/v) PEG 8000, 100 mM Tris/BICINE, pH 8.5, 30 mM MgCl2 and 30 mM CaCl2, 2mM PLP added to the protein prior to crystallization, KlaeA.00906.a.B1.PW39169 at 41.1 mg/mL. Plate: 13219, well A10 drop 2, Puck: PSL-0412, Cryo: Direct