5HGW

Crystal structure of a peptide deformylase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2015-12-14
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	116.690, 121.350, 71.290
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.600
R-factor	0.1544
Rwork	0.154
R-free	0.17840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4nt8
RMSD bond length	0.012
RMSD bond angle	1.180
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (dev_2276)

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	0.054	0.022	0.548
Rmeas	0.056	0.022	0.587
Total number of observations	739114
Number of reflections	66817	835	4842
<I/σ(I)>	29.53	115.19	4.02
Completeness [%]	99.9	99.4	99.1
Redundancy	11.1		7.75

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Rigaku ReagentsJCSG+ screen E2: 200mM ammonium sulphate, 200mM NaCl, 100mM Na-cacodylate/HCl pH 6.5; BuamA.00078.a.B1.PS02512 at 17.5 mg/ml, tray 267395 e2, puck pud2-3