1E59

E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	105
Collection date	1999-09-15
Spacegroup name	P 21 21 2
Unit cell lengths	61.249, 112.142, 40.948
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.300
R-factor	0.1552
R-free	0.21340
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e58
RMSD bond length	0.013
RMSD bond angle	0.029
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELX
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.310
High resolution limit [Å]	1.300	1.300
Rmerge	0.079 *	0.401 *
Number of reflections	68073
<I/σ(I)>	17	2.1
Completeness [%]	96.6	99.9
Redundancy	3.1 *	3.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *		100 MM TRIS-HCL (PH 8.0), 200 MM LI2SO4, 20% PEG 4000, 100 MM NAVO3

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH8.0
3	1	drop		100 (mM)
4	1	reservoir	Tris-HCl	100 (mM)	pH8.75
5	1	reservoir		200 (mM)
6	1	reservoir	PEG4000	20 (%(w/v))
7	1	reservoir		100 (mM)