5TQI

Crystal structure of a pyridoxal kinase from Burkholderia multivorans

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	2016-04-13
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	82.970, 42.490, 90.510
Unit cell angles	90.00, 115.56, 90.00

Refinement procedure

Resolution	40.826 - 1.500
R-factor	0.1386
Rwork	0.138
R-free	0.17780
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.796
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	44.900		1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.076	0.049	0.492
Number of reflections	91157
<I/σ(I)>	11.27	24.72	2.82
Completeness [%]	99.3	94.5	98.8
Redundancy	3.73
CC(1/2)	0.996	0.995	0.807

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	290	RigakuReagents JCSG+ screen, B3: 20% PEG 6000, 100 mM BICINE; BumuA.00129.a.B1.PS37843 at 18.12 mg/ml; cryo: 20% EG, 2 steps; tray 270818b3, puck fsu3-5