5KIA

Crystal structure of L-threonine 3-dehydrogenase from Burkholderia thailandensis

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	2014-11-12
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	I 41 2 2
Unit cell lengths	91.770, 91.770, 173.650
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.958 - 2.100
R-factor	0.1795
Rwork	0.175
R-free	0.22610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2dq4
RMSD bond length	0.007
RMSD bond angle	0.771
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	BALBES
Refinement software	PHENIX ((dev_2650))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.958	48.958	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.054	0.023	0.462
Rmeas	0.058	0.025	0.493
Total number of observations	181263
Number of reflections	22085	293	1601
<I/σ(I)>	25.79	61.91	4.68
Completeness [%]	99.9	95.8	100
Redundancy	8.208	6.259	8.334
CC(1/2)	0.999	0.999	0.921

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Microlytic MCSG 1 screen A10, 28% PEG 400, 200mM CaCl2, 100mM HEPES/NaOH, ButhA.10611.b.B1.PS01804 at 20mg/ml + 2.5mM NAD; cryo: direct; tray 257666a10, puck xbm5-5