3UPB

1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97850
Spacegroup name	P 21 21 21
Unit cell lengths	55.045, 86.197, 140.547
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.500
R-factor	0.15181
Rwork	0.151
R-free	0.17527
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3igx
RMSD bond length	0.022
RMSD bond angle	2.057
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	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.071	0.556
Number of reflections	106919
<I/σ(I)>	20.2	4
Completeness [%]	99.9	99.9
Redundancy	5.9	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	295	Protein: 11.2 mg/ml, 0.5 M sodium chloride, 0.01 M Tris-HCl, Screen: Pegs H1 (Qiagen), 0.2 M K/Na tartrate, 20% (w/v) PEG 3350 Crystals were soaked in a mother liquor containing 20 mM arabinose-5-phosphate for 2 hours before being flash frozen for data collection, VAPOR DIFFUSION, SITTING DROP, temperature 295K, pH 8.3