3EFP

Crystal structure of the Escherichia coli twin arginine leader peptide binding protein DmsD in a monomeric form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-08-16
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	128.020, 128.020, 78.723
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.750 - 2.010
R-factor	0.18
Rwork	0.178
R-free	0.21300
Starting model (for MR)	1s9u
RMSD bond length	0.007
RMSD bond angle	1.036
Data reduction software	d*TREK
Data scaling software	d*TREK (8.0SSI)
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.750	30.750	2.080
High resolution limit [Å]	2.010	4.330	2.010
Rmerge	0.089	0.036	0.362
Total number of observations		29169	26522
Number of reflections	48639
<I/σ(I)>		30.1	4.5
Completeness [%]	97.7	99.4	95.6
Redundancy	5.72	5.65	5.58

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	1.25M ammonium sulfate, 12% glycerol, 0.1M Bis-Tris pH 6.5, 72 hours, VAPOR DIFFUSION, HANGING DROP, temperature 291K