4WBT

Crystal structure of histidinol-phosphate aminotransferase from Sinorhizobium meliloti in complex with pyridoxal-5'-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	2014-03-20
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	131.055, 64.322, 137.048
Unit cell angles	90.00, 93.24, 90.00

Refinement procedure

Resolution	50.000 - 1.600
R-factor	0.1469
Rwork	0.146
R-free	0.16340
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.461
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.630
High resolution limit [Å]	1.600	4.340	1.600
Rmerge	0.080	0.037	0.574
Rmeas	0.085	0.048	0.625
Rpim	0.053	0.030	0.387
Total number of observations	690744
Number of reflections	150339
<I/σ(I)>	9		2.38
Completeness [%]	99.9	99.2	98.6
Redundancy	4.6	2.4	4.2
CC(1/2)		0.996	0.679

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	0.2 ul of 17.6 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the MCSG-I condition #94 (0.1 M HEPES:NaOH pH 7.5, 25% (w/v) PEG 3350) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was incubated with 1/50 v/v of 2 mg/ml chymotrypsin solution at 289 K for 3 hours.