3B3X

Crystal structure of class A beta-lactamase of Bacillus licheniformis BS3 with aminocitrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2005-03-04
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	46.665, 104.710, 63.884
Unit cell angles	90.00, 93.96, 90.00

Refinement procedure

Resolution	36.470 - 2.500
R-factor	0.223
Rwork	0.220
R-free	0.28800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1w7f
RMSD bond length	0.016
RMSD bond angle	1.834
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	63.758	36.470	2.640
High resolution limit [Å]	2.500	7.910	2.500
Rmerge	0.083	0.042	0.371
Total number of observations		1645	3926
Number of reflections	17440
<I/σ(I)>	7.6	10.8	1.9
Completeness [%]	82.3	81.2	75.5
Redundancy	1.9	2.9	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	hanging drop	7.2	293	5micro-l of a protein solution (at a concentration of 38mg/ml in 50mM NaCl, 10mM Tris buffer, pH 7.2), 4micro-l of 8% PEG 6000 in 100mM sodium aminocitrate buffer (pH 3.4) plus 1micro-l of 0.1M urea additive, equilibrated against 1ml of a 20% PEG 6000, hanging drop, temperature 293K