1K89

K89L MUTANT OF 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	1995-11-23
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	161.800, 161.800, 102.500
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.050
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CLOSTRIDIUM SYMBIOSUM GLUTAMATE DEHYDROGENASE (WILD TYPE) CRYSTALLISED WITH SODIUM GLUTAMATE IN SPACE GROUP R32. ALL WATERS AND THE BOUND GLUTAMATE SUBSTRATE REMOVED.
RMSD bond length	0.070 *
RMSD bond angle	2.200 *
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]	24.000	2.100
High resolution limit [Å]	2.050	2.050
Rmerge	0.029	0.112
Total number of observations	97593 *
Number of reflections	27219
<I/σ(I)>	17.6	6.4
Completeness [%]	84.7	72.7
Redundancy	3.6	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7		pH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	sodium glutamate	0.25 (M)
3	1	drop	sodium phosphate	0.1 (M)
4	1	drop	beta-mercaptoethanol	1 (mM)
5	1	drop	EDTA	1 (mM)
6	1	reservoir	ammonium sulfate	39.5-40.5 (%sat)