2V5B

The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	90
Detector technology	CCD
Collection date	2007-11-20
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	70.327, 77.673, 43.052
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	52.130 - 2.000
R-factor	0.2137
Rwork	0.212
R-free	0.25693
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tcd
RMSD bond length	0.021
RMSD bond angle	1.839
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER (PROGRAM OF CCP4 6)
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.130	2.020
High resolution limit [Å]	2.000	2.000
Rmerge	0.050	0.260
Number of reflections	16558
<I/σ(I)>	18.71	3.89
Completeness [%]	99.9	100
Redundancy	4.15	4.21

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	282	CRYSTALS WERE GROWN AT 9 DEGREES. RESERVOIR SOLUTION OF 100 MM HEPES, PH 7.5, 10% PEG 6000, AND 5% 2-METHYL-2,4-PENTANEDIOL. THE CRYSTALS WERE CRYOPROTECTED BY ADDING PEG 400 30% TO THE RESERVOIR. THEY WERE IMMEDIATELY FROZEN IN LIQUID NITROGEN.