1E9N

A second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	110
Detector technology	CCD
Collection date	1999-07-15
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	137.522, 45.016, 125.702
Unit cell angles	90.00, 108.03, 90.00

Refinement procedure

Resolution	20.000 - 2.200
Rwork	0.186
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	TO BE PUBLISHED
RMSD bond length	0.018
RMSD bond angle	18.920 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	EPMR
Refinement software	TNT (5F)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	67.420	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.082 *	0.379
Total number of observations	102875 *
Number of reflections	34905
<I/σ(I)>	11.8	2.1
Completeness [%]	93.0	70.5
Redundancy	2.9	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	4 *	HANGING DROP, DROP 2+2 UL, 15MG/ML PROTEIN, 1 ML WELL, 0.1M TRIS-HCL, PH 7.5, 0.2M NAOAC, 30% PEG4K, 20MM HECAMEG, 1MM PB(OAC)2, 1MM DTT

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-12 (mg/ml)
2	1	reservoir	Tris-HCl	0.1 (M)
3	1	reservoir	sodium acetate	0.2 (M)
4	1	reservoir	PEG4000	25 (%)
5	1	reservoir	lead (II) acetate	1 (mM)
6	1	reservoir	HECAMEG	19.5 (mM)