5VH6

2.6 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-406) of Elongation Factor G from Bacillus subtilis.

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	2017-03-28
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 43 21 2
Unit cell lengths	56.672, 56.672, 248.722
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.810 - 2.610
R-factor	0.22811
Rwork	0.225
R-free	0.27732
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2xex
RMSD bond length	0.006
RMSD bond angle	1.238
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.640
High resolution limit [Å]	2.600	2.600
Rmerge	0.093	0.796
Rpim	0.038	0.333
Number of reflections	13280	638
<I/σ(I)>	18.5	2.2
Completeness [%]	99.8	100
Redundancy	6.8	6.4
CC(1/2)		0.867

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	295	Protein: 8.0 mg/ml, 0.01M Tris HCl (pH 8.3); Screen: PACT (B7), 0.2M Sodium chloride, 0.1M MES pH (6.0), 20% (w/v) PEG 6000.