5T3E

Crystal structure of a nonribosomal peptide synthetase heterocyclization domain.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2015-10-07
Detector	RAYONIX MX-300
Wavelength(s)	0.97949
Spacegroup name	C 1 2 1
Unit cell lengths	139.693, 124.937, 68.925
Unit cell angles	90.00, 95.66, 90.00

Refinement procedure

Resolution	39.894 - 2.297
R-factor	0.2024
Rwork	0.201
R-free	0.23710
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jn3
RMSD bond length	0.004
RMSD bond angle	0.773
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall
Low resolution limit [Å]	39.900
High resolution limit [Å]	2.300
Number of reflections	52064
<I/σ(I)>	15.1
Completeness [%]	99.8
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	BmdB-Cy2 was crystallized by mixing with 0.88% Tween 20, 1.62 M ammonium sulfate, 0.1 M HEPES pH 7.5, 2.67% PEG 400, and 3% 6-aminohexanoic acid, and equilibrated 0.88% Tween 20, 1.62 M ammonium sulfate, 0.1 M HEPES pH 7.5, 2.67% PEG 400, and 3% 6-aminohexanoic acid. Crystals were transferred into a solution of mother liquor plus 20% (v/v) ethylene glycol, and flash-cooled in liquid nitrogen.