3CC1

CRYSTAL STRUCTURE OF A PUTATIVE ALPHA-N-ACETYLGALACTOSAMINIDASE (BH1870) FROM BACILLUS HALODURANS C-125 AT 2.00 A RESOLUTION

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2007-10-26
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.91840, 0.97953, 0.97939
Spacegroup name	P 61 2 2
Unit cell lengths	146.943, 146.943, 213.526
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	34.816 - 2.000
R-factor	0.164
Rwork	0.162
R-free	0.19000
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.548
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHELX
Refinement software	REFMAC (5.4.0067)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	34.816	34.816	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.153	0.059	1.008
Total number of observations		11193	74790
Number of reflections	91976
<I/σ(I)>	4.1	9	0.8
Completeness [%]	100.0	98.3	100
Redundancy	11	9.4	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	277	NANODROP, 0.2M (NH4)2SO4, 10.0% Glycerol, 20.0% PEG 300, 0.1M Phosphate citrate pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K