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THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION

Experimental procedure

Spacegroup name	P 1 21 1
Unit cell lengths	102.400, 68.300, 102.800
Unit cell angles	90.00, 105.60, 90.00

Refinement procedure

Resolution	? - 2.200
R-factor	0.179
Rwork	0.179
RMSD bond length	0.013
RMSD bond angle	2.840
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
High resolution limit [Å]	1.900 *
Rmerge	0.055 *
Total number of observations	208894 *
Number of reflections	80528 *
Completeness [%]	75.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	5.3 *	20 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	12 (mg/ml)
2	1	2	Tris-HCl	5 (mM)
3	1	2	beta-mercaptoethanol	1 (mM)
4	1	2		0.5 (mM)
5	1	2	EDTA	0.1 (mM)
6	1	2	PEG3350	11-12 (%(w/v))