5VCP

Crystal structure of a peptide deformylase from Burkholderia xenovorans 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	2016-02-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	63.110, 90.330, 140.210
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.536 - 1.950
R-factor	0.1625
Rwork	0.162
R-free	0.19180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5kob
RMSD bond length	0.007
RMSD bond angle	1.062
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.536	48.536	2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.040	0.021	0.530
Rmeas	0.044	0.023	0.578
Total number of observations	362861
Number of reflections	59117	711	4328
<I/σ(I)>	23.88	56.67	3.79
Completeness [%]	99.8	93.4	100
Redundancy	6.138	5.093	6.205
CC(1/2)	1.000	0.999	0.944

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	1:1 22 mg/mL BuxeA.00078.a.B1.PS37823 / Rigaku reagents Morpheus A8 (0.03 M magnesium chloride, 0.03 M calcium chloride, 0.1 M HEPES/MOPS, pH 7.5, 12.5% MPD, 12.5% PEG1000, 12.5% PEG3350), crystal id: wda5-2 270123a8