1URH

The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Collection date	2002-07-15
Spacegroup name	P 43
Unit cell lengths	150.170, 150.170, 37.930
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.800
R-factor	0.234
Rwork	0.234
R-free	0.28900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rhs
RMSD bond length	0.009
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.066	0.483
Total number of observations	312079 *
Number of reflections	21524
<I/σ(I)>	16	2
Completeness [%]	95.6 *	97.9
Redundancy	14

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *	294 *	Spallarossa, A., (2003) Acta Cryst., D59, 168. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH8.0
3	1	drop		50 (mM)
4	1	reservoir	ammonium sulfate	1.9 (M)
5	1	reservoir	MES	40 (mM)	pH6.2
6	1	reservoir	PEG400	2 (%(v/v))
7	1	reservoir		10 (mM)