2HWG

Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2000-06-01
Detector	MARRESEARCH
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	85.487, 94.084, 161.007
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.700
R-factor	0.208
Rwork	0.204
R-free	0.28400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zym 2bg5
RMSD bond length	0.018
RMSD bond angle	1.800
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.096	0.326
Number of reflections	36262
Completeness [%]	99.5	98.7
Redundancy	5.8	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	The protein sample (10 mg/mL) was mixed with MgCl2 and PEP to bring each additive to a final concentration of 10 mM. After ~5 min, sodium oxalate was added to a final concentration of 10 mM. Drops containing 1:1 protein and reservoir solution were equilibrated against reservoir solution containing 22% w/v polyethylene glycol 6000, 2% saturated ammonium sulfate, and 100 mM Na+HEPES., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K