1ONH

GC1 beta-lactamase with a penem inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-06-24
Detector	ADSC QUANTUM 210
Wavelength(s)	0.9474
Spacegroup name	P 21 21 2
Unit cell lengths	76.288, 68.873, 62.014
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.380
R-factor	0.1383
Rwork	0.135
R-free	0.20200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gce
RMSD bond length	0.010
RMSD bond angle	0.028
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.430
High resolution limit [Å]	1.380	1.380
Rmerge	0.103	0.514
Total number of observations	377696 *
Number of reflections	65047	5075 *
<I/σ(I)>	10.5	2
Completeness [%]	97.2	77
Redundancy	5.8	2.52

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	10% PEG 8000 in 50 mM HEPES over 20 % PEG, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	PEG8000	10 (%)
3	1	drop	HEPES	50 (mM)	pH7.0
4	1	reservoir	PEG	20 (%)
5	1	reservoir	HEPES	100 (mM)