1GUB

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	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Spacegroup name	P 4 3 2
Unit cell lengths	133.100, 133.100, 133.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.000 * - 3.100
R-factor	0.284
Rwork	0.280
R-free	0.27400 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rpj
RMSD bond length	0.024 *
RMSD bond angle	2.500 *
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]	29.000	3.160
High resolution limit [Å]	3.080	3.080
Rmerge	0.094 *	0.338 *
Number of reflections	625
<I/σ(I)>	7.1	2.3
Completeness [%]	99.5	99.9
Redundancy	11.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.8 *		pH 9.00

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	PEG2000MME	20-30 (%)
4	1	reservoir	Tris-HCl	0.1 (M)	pH9.0
5	1	reservoir		0.01 (M)