4JNQ

Crystal structure of a thioredoxin reductase from Brucella melitensis

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	2013-03-10
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 2 21 21
Unit cell lengths	44.790, 77.190, 104.080
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.180 - 1.800
R-factor	0.1639
Rwork	0.163
R-free	0.18460
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cl0
RMSD bond length	0.013
RMSD bond angle	1.483
Data scaling software	XSCALE
Phasing software	PHASER (2.5.2)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.051	0.023	0.481
Number of reflections	34271	444	2478
<I/σ(I)>	24.46	55.75	4
Completeness [%]	99.9	95.9	99.9
Redundancy	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	BrmeA.00058.a.A1 PS01310 at 21.1 mg/mL with 2 mM ebselen against Morpheus screen condition G1: 10% PEG20000, 20% PEG550 MME, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M trisodium citrate, 0.02 M sodium potassium L-tartrate, 0.02 M sodium oxamate, 0.1 M MES/imidazole, pH 6.5, crystal tracking ID 241371g1, unique puck ID qoj501, VAPOR DIFFUSION, SITTING DROP, temperature 289K