5UNN

Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc02828 (SmGhrA) from Sinorhizobium meliloti in apo form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2015-04-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	I 41
Unit cell lengths	128.592, 128.592, 122.847
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.1482
Rwork	0.147
R-free	0.17420
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4z0p
RMSD bond length	0.011
RMSD bond angle	1.369
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0151)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.030
High resolution limit [Å]	2.000	5.430	2.000
Rmerge	0.108	0.046	0.902
Rmeas	0.117	0.050	0.986
Rpim	0.044	0.019	0.389
Number of reflections	67353
<I/σ(I)>	6.9		1.7
Completeness [%]	100.0	99.8	100
Redundancy	6.9	6.9	6.6
CC(1/2)		0.998	0.615

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	289	0.2 ul of 12 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 suite I condition # 88 (0.1 M Sodium citrate pH=5.6, 20% v/v 2-Propanol, 20% w/v PEG 4000 ) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci)