1R2T

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]	85
Detector technology	IMAGE PLATE
Collection date	1999-03-07
Detector	MARRESEARCH
Wavelength(s)	1.31
Spacegroup name	P 21 21 21
Unit cell lengths	65.159, 72.035, 93.252
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	13.500 * - 2.250
R-factor	0.1841 *
Rwork	0.182
R-free	0.22000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hti
RMSD bond length	0.011
RMSD bond angle	1.309
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]	13.500 *	2.290
High resolution limit [Å]	2.250	2.250
Rmerge	0.107 *	0.366 *
Number of reflections	20842
<I/σ(I)>	10.16	2.63
Completeness [%]	97.5	99.7
Redundancy	2.93	2.83

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)