4PUP

2.75 Angstrom resolution crystal structure of uncharacterized protein from Burkholderia cenocepacia J2315

Experimental procedure

Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2014-02-27
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	64.785, 88.051, 79.375
Unit cell angles	90.00, 108.34, 90.00

Refinement procedure

Resolution	28.640 - 2.750
R-factor	0.22589
Rwork	0.224
R-free	0.25497
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.865
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.800
High resolution limit [Å]	2.750	2.750
Rmerge	0.111	0.605
Number of reflections	10997
<I/σ(I)>	18.9	2.2
Completeness [%]	99.6	97.3
Redundancy	5.3	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	295	protein: 7 mg/ml in 10 mM Tris-HCl pH 8.3, 500 mM NaCl, 5 mM BME, crystallization conditions: 0.2 M Sodium formate, 20 % (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K