2BFQ

MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Collection date	2004-05-02
Spacegroup name	P 61
Unit cell lengths	88.116, 88.116, 60.280
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.500
R-factor	0.2103
Rwork	0.210
R-free	0.23250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hjz
RMSD bond length	0.012
RMSD bond angle	1.590
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.440	1.580
High resolution limit [Å]	1.500	1.500
Rmerge	0.050	0.260
Number of reflections	41551
<I/σ(I)>	18.3	5.3
Completeness [%]	97.0	98.3
Redundancy	4.8	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.6		30% PEG 4000, 0.2 AMMONIUM ACETATE, 0.1 TRI SODIUM CITRATE (PH 5.6), 18MG/ML PROTEIN, 1.5 MM ADP-RIBOSE, 5MM DTT. CRYO BUFFER CONTAINED 20% GLYCEROL