6N2L

Crystal structure of a histone family protein DNA-binding protein from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2016-06-06
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	38.210, 71.400, 76.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.365 - 1.850
R-factor	0.2495
Rwork	0.245
R-free	0.29460
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1P71 as per MoRDa
RMSD bond length	0.006
RMSD bond angle	0.643
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	38.365	38.365	1.900
High resolution limit [Å]	1.850	8.270	1.850
Rmerge	0.064	0.048	0.506
Rmeas	0.066	0.050	0.537
Total number of observations	137737
Number of reflections	9290	129	667
<I/σ(I)>	28.26	56.23	4.72
Completeness [%]	99.9	100	100
Redundancy	14.826	17.24	8.852
CC(1/2)	0.998	0.996	0.969

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	6.92 mg/mL BuamA.00144.b.B1.PS37906 with Microlytic MCSG1 screen, condition B8 (25.5% PEG4000, 15% glycerol, 170 mM sodium acetate), cryoprotection: direct, tray 272705 h3, puck ndf9-5