3QH8

Crystal structure of a beta-lactamase-like protein bound to AMP from brucella melitensis, long wavelength synchrotron data

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2010-12-18
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.3476
Spacegroup name	C 2 2 21
Unit cell lengths	73.210, 75.530, 98.940
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.880 - 1.600
R-factor	0.145
Rwork	0.143
R-free	0.16600
Structure solution method	MR
Starting model (for MR)	3md7
RMSD bond length	0.015
RMSD bond angle	1.652
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.069	0.390
Number of reflections	36362
<I/σ(I)>	25.08	5.8
Completeness [%]	99.6	95.9
Redundancy	12.3	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	290	15-18% PEG 3350, 200MM K/NA TARTRATE, 100MM BISTRISPROPANE PH 8.0, BRABA.11339.A.PW27637 AT 18MG/ML SUPPLEMENTED WITH 1MM AMPPNP AND 2MM MGCL2 AT 18MG/ML. CRYO: 21% PEG 3350, 15% EG, 165MM K/NA TARTRATE, 87MM BISTRISPROPANE PH 8.0, 1MM AMPPNP, 2MM MGCL2, VAPOR DIFFUSION, SITTING DROP, temperature 290K