4Z04

Crystal structure of a probable lactoylglutathione lyase from Brucella melitensis in complex with glutathione

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	2015-03-12
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	82.630, 39.500, 41.700
Unit cell angles	90.00, 116.29, 90.00

Refinement procedure

Resolution	20.622 - 1.450
R-factor	0.1351
Rwork	0.134
R-free	0.16110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4qb5
RMSD bond length	0.006
RMSD bond angle	1.020
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]	50.000	50.000	1.490
High resolution limit [Å]	1.450	6.480	1.450
Rmerge	0.034	0.027	0.308
Rmeas	0.040	0.032	0.383
Total number of observations	84185
Number of reflections	21264	212	1427
<I/σ(I)>	20.5	39.01	2.97
Completeness [%]	98.4	78.8	89.1
Redundancy	3.96		2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Molecular Dimensions, Morpheus e4: 30mM each: Di-Ethyleneglycol, Tri-Ethyleneglycol, TetraEthyleneglycol, Penta-Ethyleneglycol; 100mM Imidazole/MES pH 6.5; 12.5% each MPD (racemic), PEG 1K, PEG 3350; BrabA.17481.b.B1.PS02324 at 21.7mg/ml with 8mM Gluathione; Cryo: direct; tray 261781e4; puck epp4-1