1GK9

Crystal structures of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MAR scanner 300 mm plate
Spacegroup name	P 1 21 1
Unit cell lengths	51.300, 131.600, 63.900
Unit cell angles	90.00, 105.90, 90.00

Refinement procedure

Resolution	20.000 - 1.300
R-factor	0.148 *
Rwork	0.148
R-free	0.16900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pnk
RMSD bond length	0.014 *
RMSD bond angle	0.027 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.310
High resolution limit [Å]	1.300	1.300
Rmerge	0.075	0.244
Total number of observations	651295 *
Number of reflections	190229
<I/σ(I)>	20.5	3.4
Completeness [%]	95.5	97.1 *
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.2 *	291 *	McVey, C.E., (1997) Acta Crystallog., D53, 777. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	MOPS	50 (mM)	pH7.2
3	1	reservoir	MOPS	50 (mM)	pH7.2
4	1	reservoir	PEG2000 MME	10-12 (%)
5	1	reservoir	ethylene glycol	20-25 (%)