1EU8

STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS

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
Detector technology	IMAGE PLATE
Collection date	1999-08-12
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	59.243, 81.526, 86.455
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.850 *
R-factor	0.199
Rwork	0.198
R-free	0.23200
RMSD bond length	0.007
RMSD bond angle	1.306 *
Data scaling software	XDS
Phasing software	SHARP
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.080 *	0.337
Number of reflections	67503 *	4665 *
<I/σ(I)>	13.42
Completeness [%]	97.7 *	87.4 *
Redundancy	2.6	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	18 *	25% POLYETHYLENE GLYCOL 4000, 0.2 M AMMONIUM SULFATE, 0.1 M NA-ACETATE, PROTEIN CONCENTRATION 6 mg/ml MIXED 1:1 WITH CRYSTALLIZATION SOLUTION, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	reservoir	PEG4000	25 (%(w/v))
3	1	reservoir	ammonium sulfate	200 (mM)
4	1	reservoir	sodium acetate	100 (mM)