5I2B

Crystal structure of a peptide deformylase from Burkholderia ambifaria with actinonin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2016-01-12
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	I 2 2 2
Unit cell lengths	38.590, 70.250, 140.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.012 - 1.700
R-factor	0.1769
Rwork	0.174
R-free	0.20450
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5hgw
RMSD bond length	0.007
RMSD bond angle	0.846
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (dev_2299)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.012	39.020	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.028	0.016	0.510
Number of reflections	21509
<I/σ(I)>	26.92	99.6	2.38
Completeness [%]	99.7	98.6	99.1
Redundancy	3.8		2.8
CC(1/2)	1.000

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Rigaku Reagents Morpheus screen E8: 12.5% PEG1000, 12.5% PEG3350, 12.5% MPD, 0.1 M MOPS/HEPES pH 7.5, 0.03M diethyleneglycol, 0.03M triethyleneglycol, 0.03M tetraethyleneglycol, 0.03M pentaethyleneglycol; BuamA.00078.a.B1.PS02512 at 17.5 mg/ml, tray 267396 e8, puck mbf3-1