4QTO

1.65 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus with BME-modified Cys289 and PEG molecule in active site

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	2014-06-16
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	224.249, 102.474, 118.178
Unit cell angles	90.00, 104.45, 90.00

Refinement procedure

Resolution	29.710 - 1.650
R-factor	0.13689
Rwork	0.136
R-free	0.15554
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4mpb
RMSD bond length	0.011
RMSD bond angle	1.643
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.082	0.631
Number of reflections	307248
<I/σ(I)>	16.7	2.5
Completeness [%]	98.6	97.5
Redundancy	4.3	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.5	295	7 mg/mL protein in 10 mM betaine (not observed in structure), 10 mM Tris-HCl, pH 8.3, 500 mM sodium chloride, 5 mM BME, crystallization: The Classics II Suite D4 (40): 0.1 M citric acid, pH 3.5, 25% w/v PEG3350, cryoprotectant: well solution, VAPOR DIFFUSION, SITTING DROP, temperature 295K