1R2S

CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE D03B-MX1
Synchrotron site	LNLS
Beamline	D03B-MX1
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1998-09-22
Detector	MARRESEARCH
Wavelength(s)	1.37
Spacegroup name	P 21 21 21
Unit cell lengths	73.229, 80.289, 174.283
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.000 * - 2.850
R-factor	0.174 *
Rwork	0.172
R-free	0.21190 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hti
RMSD bond length	0.012
RMSD bond angle	1.358
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000 *	2.920
High resolution limit [Å]	2.850	2.850
Rmerge	0.124	0.264 *
Number of reflections	20064
<I/σ(I)>	6.11	2.55
Completeness [%]	80.9	58.3
Redundancy	1.93	1.31

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	291	PEG 4000, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	24 (%(w/v))
2	1	reservoir		0.2 (M)
3	1	reservoir	Tris-HCl	0.1 (M)	pH8.5
4	1	reservoir	DMSO	1.1 (M)
5	1	drop	protein	10 (mg/ml)