4Q14

Crystal structure of 5-hydroxyisourate hydrolase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2014-03-30
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	P 65 2 2
Unit cell lengths	83.190, 83.190, 153.110
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	32.594 - 1.700
R-factor	0.158
Rwork	0.157
R-free	0.17780
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	used Balbes for initial refinement Balbes uses pdb entry 2h0e
RMSD bond length	0.007
RMSD bond angle	1.189
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.6)
Refinement software	PHENIX (dev_1659)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.070	0.039	0.534
Number of reflections	34159	479	2436
<I/σ(I)>	22.84	44.7	4.73
Completeness [%]	96.8	94.5	95.4
Redundancy	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	290	RigakuReagents JCSG+ screen, C2: 20% PEG 6000, 1000mM LiCl, 100mM Sodium citrate tribasic/Citric acid pH 4.0; BrmeA.17772.a.A1.PS01080 at 53.3 mg/ml, cryo 20% EG in 2 steps, tray 253210c2, puck rjo4-1, VAPOR DIFFUSION, SITTING DROP, temperature 290K