1HD7

A Second Divalent Metal Ion in the Active Site of a New Crystal Form of Human Apurinic/Apyridinimic Endonuclease, Ape1, and its Implications for the Catalytic Mechanism

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL1-5
Synchrotron site	SSRL
Beamline	BL1-5
Temperature [K]	110
Detector technology	CCD
Collection date	1999-03-15
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	128.390, 44.850, 78.140
Unit cell angles	90.00, 124.54, 90.00

Refinement procedure

Resolution	25.000 - 1.950
R-factor	0.205 *
Rwork	0.205
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	TO BE PUBLISHED
RMSD bond length	0.016
RMSD bond angle	0.038
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	EPMR
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.010
High resolution limit [Å]	1.950	1.950
Rmerge	0.074 *	0.471 *
Total number of observations	91465 *
Number of reflections	34905
<I/σ(I)>	6.6	1.5
Completeness [%]	99.4	99.3 *
Redundancy	3.3	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6 *	4 *	0.1M NAOAC PH 4.6, 25% PEG 4K, 1 MM PB(II)OAC, 10-12 MG/ML PROTEIN.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-12 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)
3	1	reservoir	PEG4000	25 (%(w/v))
4	1	reservoir	lead (II) acetate	1 (mM)