6BWT

2.45 Angstrom Resolution Crystal Structure Thioredoxin Reductase from Francisella tularensis.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-E
Synchrotron site	APS
Beamline	21-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2010-07-17
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	58.299, 112.587, 167.044
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.520 - 2.450
R-factor	0.21708
Rwork	0.215
R-free	0.25217
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tde
RMSD bond length	0.008
RMSD bond angle	1.265
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.490
High resolution limit [Å]	2.450	2.450
Rmerge	0.060	0.730
Rmeas	0.067	0.818
Rpim	0.029	0.363
Number of reflections	41167	2009
<I/σ(I)>	25.6	2.2
Completeness [%]	100.0	100
Redundancy	5	4.9
CC(1/2)		0.717

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	Protein: 7.7 mG/mL, 0.25M Sodium chloride, 0.01M Tris-HCL pH 8.3; Screen: Clssics II (F8), 0.2M Ammonium sulfate, 0.1M HEPES (pH 7.5), 25% (w/v) PEG 3350