3PY5

Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2010-12-03
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	72.850, 75.200, 98.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.210 - 1.700
R-factor	0.164
Rwork	0.163
R-free	0.19600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3md7
RMSD bond length	0.015
RMSD bond angle	1.639
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.740
High resolution limit [Å]	1.700	1.700
Rmerge	0.041	0.203
Number of reflections	29964
<I/σ(I)>	35.24	7.7
Completeness [%]	99.5	93.6
Redundancy	9.1	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	290	5-18% 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