1AUP

GLUTAMATE DEHYDROGENASE

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1993-10-12
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	162.900, 162.900, 100.700
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	18.000 - 2.500
Rwork	0.190
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CLOSTRIDIUM SYMBIOSUM GLUTAMATE DEHYDROGENASE (WILD TYPE) CRYSTALLIZED WITH SODIUM GLUTAMATE IN SPACE GROUP R32. ALL WATERS AND THE BOUND GLUTAMATE SUBSTRATE REMOVED.
RMSD bond length	0.017
RMSD bond angle	18.600 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	TFFC
Refinement software	TNT (5E)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.000	2.570
High resolution limit [Å]	2.500	2.500
Rmerge	0.070 *	0.310
Total number of observations	90734 *
Number of reflections	17791
<I/σ(I)>	9.5	2.4
Completeness [%]	99.0	99
Redundancy	5.1	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.3 *		pH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium glutamate	1.0 (M)
3	1	drop	potassium phosphate	0.1 (M)
4	1	reservoir	potassium phosphate	0.1 (M)
5	1	reservoir	ammonium sulfate	38-46 (%)