1TDF

CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE REFINED AT 2 ANGSTROM RESOLUTION: IMPLICATIONS FOR A LARGE CONFORMATIONAL CHANGE DURING CATALYSIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Spacegroup name	P 63 2 2
Unit cell lengths	123.800, 123.800, 81.560
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.300
R-factor	0.179
Rwork	0.179
RMSD bond length	0.009
RMSD bond angle	2.300
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	2.300 *
Rmerge	0.056 *
Total number of observations	54650 *
Number of reflections	17238 *
Completeness [%]	94.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *			'Kuriyan, J.', (1989) J. Biol. Chem., 264, 12752. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3300	35 (%)
2	1	reservoir	ammonium sulfate	200 (mM)	or 200 mM lithium sulfate
3	1	reservoir	MES	50 (mM)
4	1	drop	protein	20 (mg/ml)
5	1	drop	dithiothreitol	60 (mM)