4IL0

Crystal structure of GlucDRP from E. coli K-12 MG1655 (EFI target EFI-506058)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2012-12-12
Detector	RAYONIX MX-300
Wavelength(s)	0.978590
Spacegroup name	P 1
Unit cell lengths	86.090, 94.030, 155.200
Unit cell angles	101.47, 96.74, 79.86

Refinement procedure

Resolution	19.860 - 2.800
R-factor	0.1762
Rwork	0.173
R-free	0.23130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gyp
RMSD bond length	0.009
RMSD bond angle	1.253
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.8_1066)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.000	30.000	2.870
High resolution limit [Å]	2.800	12.520	2.800
Rmerge	0.143	0.033	0.539
Number of reflections	112207	938	8417
<I/σ(I)>	9.47	28.88	2.33
Completeness [%]	97.3	72.7	97.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	282	Protein solution was at 20 mg/mL containing 50 mM Tris (pH 7.5), 100 mM NaCl, 10 mM EDTA and 10 mM bME. Mother liqueur contained 0.2 M Na citrate (pH 4.6), 20% PEG 3,350. 20% glycerol was used as the cryoprotectant, vapor diffusion, hanging drop, temperature 282K