5UOG

Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc04462 (SmGhrB) from Sinorhizobium meliloti in apo form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-11-08
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97924
Spacegroup name	H 3
Unit cell lengths	176.583, 176.583, 135.008
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	36.780 - 2.400
R-factor	0.1381
Rwork	0.136
R-free	0.19040
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5j23
RMSD bond length	0.009
RMSD bond angle	1.319
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.440
High resolution limit [Å]	2.400	6.510	2.400
Rmerge	0.061	0.035	0.630
Rmeas	0.073	0.042	0.761
Rpim	0.040	0.023	0.422
Number of reflections	61899		3113
<I/σ(I)>	9.8		2
Completeness [%]	100.0	99.3	100
Redundancy	3.2	3.2	3.2
CC(1/2)		0.996	0.685

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.5	289	0.2 ul of 14 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide, 0.5 mM TCEP and 5 mM NADPH were mixed with 0.2 ul of the MCSG Suite 3 condition #61 (0.1 M Citric acid pH=3.5, 2 M Ammonium sulfate) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). The protein was crystallized with the His-tag