1GHP

STRUCTURES OF THE ACYL-ENZYME COMPLEX OF THE STAPHYLOCOCCUS AUREUS BETA-LACTAMASE MUTANT GLU166ASP:ASN170GLN WITH DEGRADED BENZYLPENICILLIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	1998-01-15
Detector	BRANDEIS - B1
Spacegroup name	I 2 2 2
Unit cell lengths	52.900, 89.700, 138.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.760
R-factor	0.185
Rwork	0.185
R-free	0.26400
Structure solution method	OTHER
Starting model (for MR)	1djc
RMSD bond length	0.017
RMSD bond angle	1.900
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	X-PLOR (3.7)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	21.800	1.820
High resolution limit [Å]	1.760	1.760
Rmerge	0.053	0.109
Number of reflections	29494	2061 *
<I/σ(I)>	17.9	2.2
Completeness [%]	86.6	63
Redundancy	2.8	2.78

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8		drop consists of equal amounts of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	10 (mg/ml)
2	1	reservoir	ammonium sulfate	89 (%sat)
3	1	reservoir	PEG2000	0.5 (%)
4	1	reservoir	sodium bicarbonate	0.1 (M)