1GUD

Hinge-bending motion of D-allose binding protein from Escherichia coli: three open conformations

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	2000-12-15
Spacegroup name	P 21 21 21
Unit cell lengths	60.229, 64.096, 142.113
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.580 * - 1.710
R-factor	0.173
Rwork	0.172
R-free	0.20800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rpj
RMSD bond length	0.025 *
RMSD bond angle	2.100 *
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.580	1.760
High resolution limit [Å]	1.710	1.700
Rmerge	0.093 *	0.362 *
Number of reflections	8404
<I/σ(I)>	13.9	6.3
Completeness [%]	100.0	100
Redundancy	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.8 *		pH 8.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop	HEPES	10 (mM)	pH7.8
3	1	reservoir	PEG4000	30 (%)
4	1	reservoir	Tris-HCl	0.1 (M)
5	1	reservoir		5 (mM)