1XLM

D254E, D256E MUTANT OF D-XYLOSE ISOMERASE COMPLEXED WITH AL3 AND XYLITOL

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	RIGAKU
Spacegroup name	C 2 2 2
Unit cell lengths	139.600, 140.700, 83.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.400
R-factor	0.1792
Rwork	0.179
R-free	0.22230 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xla
RMSD bond length	0.014
RMSD bond angle	21.300 *
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000	2.480
High resolution limit [Å]	2.400	2.400
Rmerge	0.119 *	0.520
Total number of observations	142427 *
Number of reflections	32570
<I/σ(I)>	4.87	1.1
Completeness [%]	97.0	98
Redundancy	4.4	2.65

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7		PROTEIN WAS CRYSTALLIZED FROM 0.75 M (NH4)2SO4, 1.50 MM THYMOL, 0.05 TRIS, PH 7.0, THEN SOAKED INTO A SOLUTION CONTAINING 5 MM AL3+, 1.5 M XYLITOL, 1.50 M (NH4)2SO4 AND 6.0 M THYMOL IN 1.50 M TRIS-HCL PH 8.0 FOR TWO DAYS

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.0 (mg/ml)
2	1	drop	Tris	0.05 (M)
3	1	drop	ammonium sulfate	0.75 (M)
4	1	drop	thymol	1.50 (mM)