1I45

YEAST TRIOSEPHOSPHATE ISOMERASE (MUTANT)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-05-10
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	60.601, 97.058, 49.245
Unit cell angles	90.00, 91.70, 90.00

Refinement procedure

Resolution	29.750 - 1.800
R-factor	0.175
Rwork	0.175
R-free	0.20800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ypi
RMSD bond length	0.005
RMSD bond angle	1.200
Data scaling software	SCALEPACK
Phasing software	COMO
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.073 *	0.305
Total number of observations	152637 *
Number of reflections	50459 *
<I/σ(I)>	44.2
Completeness [%]	95.2	82.4
Redundancy	2.9	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	6.8	293	16% PEG 4000, 50mM Tris, 50mM NaCl, pH 6.8, batch at 293 K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	40 (mg/ml)
2	1	1	Tris-HCl	50 (mM)
3	1	1		50 (mM)
4	1	1	EDTA	1 (mM)	pH6.8
5	1	1	PEG4000	14-16 (%)