4M54

The structure of the staphyloferrin B precursor biosynthetic enzyme SbnB bound to N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid and NADH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-18
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 41 21 2
Unit cell lengths	63.116, 63.116, 159.413
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.726 - 2.360
R-factor	0.2269
Rwork	0.223
R-free	0.25810
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.703
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHENIX (1.8.2-1309)
Refinement software	PHENIX (1.8.2-1309)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.730	50.000	2.400
High resolution limit [Å]	2.360	6.400	2.360
Rmerge	0.126	0.055	0.590
Number of reflections	13956
<I/σ(I)>	6.5
Completeness [%]	99.4	96.8	98.7
Redundancy	6.9	8.1	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	0.1 M Hepes, 0.2 M MgCl2, 29-33% PEG 400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K