6CAZ

Crystal structure of a peptide deformylase from Legionella pneumophila

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2018-01-14
Detector	RIGAKU SATURN 944
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	38.210, 50.900, 105.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.829 - 1.500
R-factor	0.1673
Rwork	0.166
R-free	0.19290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2w3t
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	45.829	45.829	1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.036	0.026	0.392
Rmeas	0.037	0.027	0.424
Number of reflections	33486	449	2368
<I/σ(I)>	33.45	99.87	4.74
Completeness [%]	99.3	99.6	96.3
Redundancy	10.049	17.753	6.825
CC(1/2)	1.000	0.999	0.877

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	16.5 mg/mL LepnA.00882.a.B1.P38390 against Morpheus screen condition F1 10% PEG 10,000, 20% PEG 550 MME, 0.02 M each monosaccharide (D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-glucosamine), 0.1 M MES/imidazole pH 6.5, crystal tracking ID 297178f1, ugh2-12