1M6J

CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	103
Detector technology	IMAGE PLATE
Collection date	1999-10-19
Detector	MARRESEARCH
Wavelength(s)	0.782
Spacegroup name	P 21 21 2
Unit cell lengths	85.729, 119.947, 50.392
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 * - 1.500
R-factor	0.184
Rwork	0.184
R-free	0.20700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5tim
RMSD bond length	0.004
RMSD bond angle	21.500 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((TRUNCATE))
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	69.750	1.590
High resolution limit [Å]	1.500	1.500
Rmerge	0.040 *
Total number of observations	360647 *
Number of reflections	80420 *
<I/σ(I)>	15.7
Completeness [%]	99.4 *	76.1
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	18 *	28% PEG 1500, 30% 1,6-hexanediol, pH 7.0, VAPOR DIFFUSION, HANGING DROP at 291K, temperature 291.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	PEG1500	28 (%(w/v))
3	1	reservoir	1,6-hexanediol	30 (%(v/v))