1BVU

GLUTAMATE DEHYDROGENASE FROM THERMOCOCCUS LITORALIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	293
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	141.900, 197.500, 125.700
Unit cell angles	90.00, 113.60, 90.00

Refinement procedure

Resolution	10.000 - 2.500
Structure solution method	MIR
RMSD bond length	0.013
RMSD bond angle	1.530
Data reduction software	MOSFLM
Data scaling software	CCP4 ((ROTAVATA))
Phasing software	MLPHARE
Refinement software	TNT

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.500
Rmerge	0.042
Total number of observations	173711 *
Number of reflections	101702
Completeness [%]	93.0
Redundancy	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8		35MG/ML PROTEIN IN 0.1M HEPES BUFFER PH 8.0 CONTAINING 1.7-1.8M AMMONIUM SULPHATE AND 1.5% W/V PEG 8000.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	35 (mg/ml)
2	1	reservoir	HEPES	0.1 (M)
3	1	reservoir	ammonium sulfate	1.7-1.8 (M)
4	1	reservoir	PEG8000	1.5 (%(w/v))