1NRF

C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-09-07
Detector	MARRESEARCH
Wavelength(s)	0.9786
Spacegroup name	P 41
Unit cell lengths	45.848, 45.848, 130.198
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.500 * - 2.500
Rwork	0.204
R-free	0.25700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Class D beta-lactamase OXA-2 from Salmonella typhimurium
RMSD bond length	0.007
RMSD bond angle	23.100 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.440 *	2.500
High resolution limit [Å]	2.440	2.440
Rmerge	0.068 *	0.232
Number of reflections	9979	745 *
<I/σ(I)>	8.9	3.7
Completeness [%]	99.7	99.9 *
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.95	293	18% PEG 8000, 5% Glycerol, 50mM CaCl2 in 0.1M Cacodylate, pH 6.95, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG8000	18 (%)
3	1	reservoir	glycerol	5 (%)
4	1	reservoir		50 (mM)
5	1	reservoir	cacodylate	0.1 (M)	pH6.95