1KN0

Crystal Structure of the human Rad52 protein

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL45PX
Synchrotron site	SPring-8
Beamline	BL45PX
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-04-27
Detector	RIGAKU RAXIS
Wavelength(s)	0.979, 0.9795, 1.02
Spacegroup name	P 43 21 2
Unit cell lengths	145.610, 145.610, 247.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.850
R-factor	0.2361
Rwork	0.231
R-free	0.29700
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	1.250 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.900
High resolution limit [Å]	2.850	2.850
Rmerge	0.073 *	0.404 *
Total number of observations	1378830 *
Number of reflections	63100 *
Completeness [%]	99.7	99.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.2	20 *	PEG 5000MME, ammonium sulfate, sodium cacodylate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3-3.5 (mg/ml)
2	1	drop	PEG5000 MME	12 (%)
3	1	drop	ammonium sulfate	80 (mM)
4	1	drop	betaine monohydrate	20 (mM)	or urea
5	1	drop	sodium cacodylate	40 (mM)	pH6.2
6	1	reservoir	PEG5000 MME	15 (%)
7	1	reservoir	ammonium sulfate	0.1 (M)
8	1	reservoir	sodium cacodylate	50 (mM)	pH6.2