5KOB

Crystal structure of a peptide deformylase from Burkholderia xenovorans

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	2016-03-31
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	63.550, 92.000, 142.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.072 - 1.600
R-factor	0.1652
Rwork	0.165
R-free	0.19190
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5ghw
RMSD bond length	0.006
RMSD bond angle	0.873
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((dev_2443: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.640
High resolution limit [Å]	1.600	7.160	1.600
Rmerge	0.050	0.032	0.508
Number of reflections	109668
<I/σ(I)>	17.52	39.56	2.89
Completeness [%]	99.3	90.9	100
Redundancy	5.5		5.5
CC(1/2)	0.999	0.998	0.892

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	JCSG+ A5 (270125a5): 20% w/v PEG3350, 200mM Magnesium formate dihydrate; 20eg2step; protein 22mg/mL; ehj6-10