4MAD

Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44XU
Synchrotron site	SPring-8
Beamline	BL44XU
Temperature [K]	100
Detector technology	CCD
Collection date	2012-04-09
Detector	BRUKER SMART 6500
Wavelength(s)	0.9
Spacegroup name	C 1 2 1
Unit cell lengths	143.268, 93.122, 119.567
Unit cell angles	90.00, 125.67, 90.00

Refinement procedure

Resolution	41.660 - 1.800
R-factor	0.1829
Rwork	0.181
R-free	0.21560
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3d3a
RMSD bond length	0.008
RMSD bond angle	1.051
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (refmac_5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.830
High resolution limit [Å]	1.800	4.880	1.800
Rmerge	0.109	0.066	0.520
Number of reflections	117585
<I/σ(I)>	24.672
Completeness [%]	99.6	99.1	99.5
Redundancy	10.5	10.4	10.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	10mg/ml Protein in 10mM Tris-HCl and 1mM EDTA (pH 7.5), Reservoir (20% (w/v) PEG 6000, 100mM HEPES, 0.2M NaCl, pH 7.0), Protein:Reservoir=1:1 , VAPOR DIFFUSION, SITTING DROP, temperature 277K