5TY0

2.22 Angstrom Crystal Structure of N-terminal Fragment (residues 1-419) of Elongation Factor G from Legionella pneumophila.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2016-11-15
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	53.399, 89.853, 117.980
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.870 - 2.220
R-factor	0.16625
Rwork	0.165
R-free	0.19546
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4fn5
RMSD bond length	0.009
RMSD bond angle	1.444
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	REFMAC (5.8.0155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.260
High resolution limit [Å]	2.220	2.220
Rmerge	0.080	0.659
Number of reflections	28863
<I/σ(I)>	24.1	3.2
Completeness [%]	99.9	99.4
Redundancy	7.3	7.4
CC(1/2)		0.861

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Protein: 9.4 mg/ml, 0.01M Tris HCl (pH 8.3); Screen: JCSG+ (C4), 0.1M HEPES (pH 6.5), 10% (w/v) PEG 6000; Cryo: Screen solution + 50% Sucrose, (1:1)