1ELJ

THE CRYSTAL STRUCTURE OF LIGANDED MALTODEXTRIN-BINDING PROTEIN FROM PYROCOCCUS FURIOSUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-10-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	61.118, 68.832, 127.726
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	100.000 - 1.850
R-factor	0.1842
Rwork	0.196
R-free	0.22890
RMSD bond length	0.070
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.053 *	0.230
Number of reflections	42983 *
<I/σ(I)>	20.08
Completeness [%]	91.9 *	84.9
Redundancy	4.5	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	298	reservoir: 2.4 M ammonium sulfate, 0.1 M bicine-hcl. drop: 6 mg/ml protein 1:1 with reservoir, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	reservoir	ammonium sulfate	2.4 (M)
3	1	reservoir	bicine	0.1 (M)
4	1	reservoir	beta-mercaptoethanol	0.1 (%(v/v))