1L1O

Structure of the human Replication Protein A (RPA) trimerization core

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-05
Detector	ADSC QUANTUM 4
Wavelength(s)	1.008
Spacegroup name	P 31 2 1
Unit cell lengths	88.527, 88.527, 341.090
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.920 - 2.800
R-factor	0.236
Rwork	0.236
R-free	0.28300 *
Structure solution method	MAD
RMSD bond length	0.019 *
RMSD bond angle	25.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.062 *	0.532 *
Total number of observations	233991 *
Number of reflections	43573
<I/σ(I)>	2.7	2.7
Completeness [%]	99.2	99.7
Redundancy	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8	300	Bochkareva, E., (2000) J.Biol.Chem., 275, 27332. *
1	VAPOR DIFFUSION, SITTING DROP	7.8	300	Bochkareva, E., (2000) J.Biol.Chem., 275, 27332. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES	0.1 (M)	pH7.8
2	1	reservoir	glycerol	9 (%)
3	1	reservoir	ammonium sulfate	1.6 (M)