1AKE

STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP5A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE

Experimental procedure

Spacegroup name	P 21 2 21
Unit cell lengths	73.200, 79.800, 85.000
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.900 *
R-factor	0.196
Rwork	0.196
RMSD bond length	0.016
RMSD bond angle	3.200
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	9999.000 *
High resolution limit [Å]	1.850 *	1.850 *
Rmerge	0.147 *	0.805 *
Total number of observations	156159 *
Number of reflections	40700 *	7170 *
Completeness [%]	94.1 *	92.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.7 *	20 *	referred to J.Mol.Biol. 202.909-912 1988 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20-25 (mg/ml)
2	1	drop	Ap5A	2 (mM)
3	1	drop	MES	50 (mM)
4	1	drop	PEG1500	1.5 (%(w/v))
5	1	drop	ammonium sulfate	1.5 (M)
6	1	reservoir	MES	50 (mM)
7	1	reservoir	ammonium sulfate	2.0-2.2 (M)