4QYB

2.1 Angstrom resolution crystal structure of uncharacterized protein, disulfide-bridged dimer, from Burkholderia cenocepacia J2315

Experimental procedure

Experimental method	SINGLE WAVELENGTH
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	2014-07-21
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	I 2 2 2
Unit cell lengths	64.945, 85.634, 93.669
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.900 - 2.100
R-factor	0.21315
Rwork	0.211
R-free	0.25648
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4pup
RMSD bond length	0.012
RMSD bond angle	1.569
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.063	0.410
Number of reflections	14651
<I/σ(I)>	49.5	5.3
Completeness [%]	95.1	100
Redundancy	7.2	7.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	295	protein - 9.6 mg/mL in 10 mM Tris-HCl pH 8.3, 250 mM NaCl, 5 mM BME, crystallization - The Classics II Suite C4 (28): 560 mM Sodium citrate pH 7.0, cryo - 25% (v/v) sucrose, VAPOR DIFFUSION, SITTING DROP, temperature 295K