4E0C

1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)

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	2012-02-09
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	54.761, 87.019, 140.688
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.590 - 1.800
R-factor	0.15254
Rwork	0.151
R-free	0.18917
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3igx
RMSD bond length	0.020
RMSD bond angle	1.948
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	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.077	0.491
Number of reflections	62204
<I/σ(I)>	20.5	4
Completeness [%]	98.5	99.4
Redundancy	6.6	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	295	Protein: 11.2 mg/ml, 0.5 M sodium chloride, 0.01 M Tris-HCl (pH 8.3), Screen: Pegs G1 (Qiagen), 0.2 M magnesium chloride, 20% (w/v) Peg 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K