1F05

CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	103
Detector technology	IMAGE PLATE
Collection date	1999-02-06
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	45.570, 113.570, 69.190
Unit cell angles	90.00, 101.37, 90.00

Refinement procedure

Resolution	19.900 - 2.450
R-factor	0.225
Rwork	0.225
R-free	0.25800
Starting model (for MR)	1onr Escherichia coli Transaldolase B
RMSD bond length	0.006
RMSD bond angle	20.600 *
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.970	2.570
High resolution limit [Å]	2.440	2.440
Rmerge	0.080 *	0.206 *
Total number of observations	60447 *
Number of reflections	22520
<I/σ(I)>	7.4
Completeness [%]	88.2	79.7
Redundancy	2.7	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	293	drop consists of equal volume of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	Tris-HCl	50 (M)
3	1	reservoir	PEG4000	27 (%(w/v))
4	1	reservoir		0.08 (%)
5	1	reservoir		0.3 (M)