5T8Z

Crystal structure of a peptide deformylase from Burkholderia multivorans in complex with actinonin

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	2016-06-22
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	I 2 2 2
Unit cell lengths	39.120, 70.540, 140.510
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.019 - 1.850
R-factor	0.1689
Rwork	0.165
R-free	0.20320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5hgw
RMSD bond length	0.010
RMSD bond angle	0.997
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.019		1.900
High resolution limit [Å]	1.850	8.270	1.850
Rmerge	0.047	0.029	0.485
Rmeas	0.051	0.032	0.522
Total number of observations	123609
Number of reflections	17066	225	1219
<I/σ(I)>	22.71	45.21	3.88
Completeness [%]	99.9	96.2	99.9
CC(1/2)	0.999	0.999	0.951

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	MCSG1 F4 (272591f4): 40% (v/v) PEG 400, 200 mM Magnesium chloride, 100 mM Sodium citrate:citric acid pH 5.5, 3 mM actinonin; direct cryo; puck kur4-4