4O0K

Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from Brucella melitensis with covalently bound substrate

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	2013-10-03
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 63 2 2
Unit cell lengths	95.280, 95.280, 125.250
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.500
R-factor	0.1593
Rwork	0.158
R-free	0.17700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4mpq
RMSD bond length	0.016
RMSD bond angle	1.683
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.066	0.047	0.518
Number of reflections	54188	716	3929
<I/σ(I)>	17.11	34.35	4.14
Completeness [%]	99.9	97	100
Redundancy	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	EmeraldBio MCSG1 screen, a11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH; crystals soaked over night with 20mM pyruvate; cryo 20% EG; BrmeB.01563.a.B1.PS01874 at 19.3mg/ml, tray 247709a11, puck amw3-4, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K