3NRH

Crystal Structure of protein BF1032 from Bacteroides fragilis, Northeast Structural Genomics Consortium Target BfR309

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2010-06-04
Detector	MAR CCD 165 mm
Wavelength(s)	0.97907
Spacegroup name	P 43 21 2
Unit cell lengths	67.442, 67.442, 157.063
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.930 - 1.800
R-factor	0.198
Rwork	0.196
R-free	0.22400
Structure solution method	SAD
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SHELX (then SOLVE/RESOLVE)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.089	0.464
Number of reflections	63917
<I/σ(I)>	34.5	3.7
Completeness [%]	99.8	99.4
Redundancy	7.3	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microbatch under oil	7.5	291	Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5) . Reservoir solution: 0.1M HEPES (pH 7.5), 12% PEG 20K, and 0.1M NH4H2PO4. , Microbatch under oil, temperature 291K