2GAR

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 21 21 21
Unit cell lengths	45.800, 47.800, 107.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.201
Rwork	0.201
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gar
RMSD bond length	0.010
RMSD bond angle	26.200 *
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	1.840
High resolution limit [Å]	1.800	1.800
Rmerge	0.050	0.287
Total number of observations	87331 *
Number of reflections	21864
<I/σ(I)>	26.3	3.1
Completeness [%]	97.0	77.6
Redundancy	4	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	3.5	22 *	CRYSTAL GREW FROM A SOLUTION OF 2%(V/V) 15% (W/V) PEG 1500, PH 3.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG1500	15 (%(w/v))