3K0K

Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-07-15
Detector	MAR scanner 300 mm plate
Wavelength(s)	0.97934
Spacegroup name	P 61 2 2
Unit cell lengths	114.422, 114.422, 123.005
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.830 - 2.700
R-factor	0.261
Rwork	0.259
R-free	0.29900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.035
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.800
High resolution limit [Å]	2.700	5.810	2.700
Rmerge	0.061	0.034	0.557
Number of reflections	13551
<I/σ(I)>	12.5
Completeness [%]	99.3	99.5	94
Redundancy	19.2	19.3	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.3	298	Li2SO4, Tris-HCl, NiCl2, pH 7.3, VAPOR DIFFUSION, temperature 298K