4N0W

X-ray crystal structure of a serine hydroxymethyltransferase from Burkholderia cenocepacia with covalently attached pyridoxal phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2013-08-08
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	65.580, 178.650, 75.660
Unit cell angles	90.00, 114.70, 90.00

Refinement procedure

Resolution	45.050 - 1.650
R-factor	0.157
Rwork	0.156
R-free	0.17510
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4mso
RMSD bond length	0.010
RMSD bond angle	1.430
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.7.0032)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.056	0.023	0.547
Number of reflections	188538	2117	13619
<I/σ(I)>	14.81	38.67	2.25
Completeness [%]	99.6	97.2	97.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	MCSG1 F11: 0.2 M ammonium sulfate, 0.1 M HEPES pH 7.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K