4P29

Crystal structure of the LpoA N-terminal domain from Haemophilus influenzae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 5ID-B
Synchrotron site	APS
Beamline	5ID-B
Temperature [K]	165
Detector technology	CCD
Collection date	2003-11-05
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97930
Spacegroup name	P 21 21 21
Unit cell lengths	48.030, 51.180, 198.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.491 - 1.950
R-factor	0.185541194582
Rwork	0.184
R-free	0.21849
Structure solution method	MIR
RMSD bond length	0.005
RMSD bond angle	0.720
Data scaling software	d*TREK (9.3D)
Phasing software	SOLVE (2.05)
Refinement software	PHENIX (dev_1888)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.240	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.074	0.390
Number of reflections	68183
<I/σ(I)>	10.4	3.1
Completeness [%]	98.8	100
Redundancy	5.42	4.71

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	295	Drop contained 2 microliters protein and 2 microliters precipitant, and reservoir contained 1 ml of precipitant. Protein:10 mg/ml SeMet-containing LpoA(33-253) in 20 mM Tris-HCl pH 8.0, 0.1 % beta-mercaptoethanol, 1 mM EDTA, 0.1 mM benzamidine. Precipitant: 0.1 M MES pH 6.5, 0.2 M ammonium sulfate, 30% polyethylene monomethyl ether 5000. Cryoprotectant: 10% glycerol in precipitant solution