1LK5

Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	0.9326
Spacegroup name	P 21 21 21
Unit cell lengths	73.548, 114.932, 119.017
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.750
R-factor	0.192
Rwork	0.191
R-free	0.24100 *
Structure solution method	MIR
RMSD bond length	0.005 *
RMSD bond angle	1.310 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	MLPHARE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.830
High resolution limit [Å]	1.750	1.750
Rmerge	0.045 *	0.239 *
Number of reflections	100845
Completeness [%]	98.9	98.9 *
Redundancy	3.7 *	2.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	20 *	0.1M HEPES-Na buffer, 0.8M Na-phosphate, 0.8M K-phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
1	VAPOR DIFFUSION, HANGING DROP	8 *	20 *	0.1M HEPES-Na buffer, 0.8M Na-phosphate, 0.8M K-phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH8.0
3	1	drop		150 (mM)
4	1	reservoir	HEPES-Na buffer	0.1 (M)	pH7.5
5	1	reservoir	sodium phosphate	0.8 (M)
6	1	reservoir	potassium phosphate	0.8 (M)