3GAR

A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	1997-03
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	50.400, 50.400, 275.500
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.900
R-factor	0.215
Rwork	0.215
R-free	0.27400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gar
RMSD bond length	0.006
RMSD bond angle	26.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.970
High resolution limit [Å]	1.800	1.900
Rmerge	0.050	0.331
Total number of observations	67156 *
Number of reflections	16340
<I/σ(I)>	22.6	2.6
Completeness [%]	92.8	81.8
Redundancy	4.1	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5	22 *	CRYSTAL GREW FROM A SOLUTION OF 2%(V/V) PEG 400. 2.0M AMMONIUM SULFATE, 0.1M HEPES, PH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG400	2 (%(v/v))
3	1	reservoir	ammonium sulfate	2.0 (M)
4	1	reservoir	sodium HEPES	0.1 (M)