5J46

Crystal structure of a Peptide Deformylase from Burkholderia multivorans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2016-03-17
Detector	RAYONIX MX-300
Wavelength(s)	0.97857
Spacegroup name	C 2 2 21
Unit cell lengths	41.720, 69.070, 119.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.923 - 1.950
R-factor	0.1769
Rwork	0.173
R-free	0.20680
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2w3t
RMSD bond length	0.007
RMSD bond angle	0.841
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.066	0.037	0.497
Number of reflections	12954
<I/σ(I)>	16.64	30.8	3.56
Completeness [%]	99.4	95.4	100
Redundancy	6.7		6.9
CC(1/2)	0.999

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	BumuA.00078.a.B1.PS37840 at 14mg/ml, mixed 1:1 with MCSG1(b5), 0.2M MgCl2, 0.1M Tris HCl pH 8.5, 25% (w/v) PEG 3350, cryo protected with 20% EG in 2 steps