3TNO

1.65 Angstrom Resolution Crystal Structure of Transaldolase B (TalA) from Francisella tularensis in Covalent Complex with Sedoheptulose-7-Phosphate

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	2011-08-17
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	56.316, 74.091, 165.423
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.990 - 1.650
R-factor	0.17406
Rwork	0.173
R-free	0.20330
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3igx
RMSD bond length	0.005
RMSD bond angle	1.069
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.068	0.538
Number of reflections	84128
<I/σ(I)>	28.9	4.3
Completeness [%]	100.0	100
Redundancy	7.3	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	295	Protein: 11.2 mg/ml, 0.5 M sodium chloride, 0.01 M Tris-HCl (pH 8.3), 0.002 M Sedoheptulose-7-phosphate, Screen: Pegs C2 (Qiagen), 0.1 M Sodium Acetate, 25% (w/v) Peg 4000, VAPOR DIFFUSION, SITTING DROP, temperature 295K