1H2G

Altered substrate specificity mutant of penicillin acylase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	120
Detector technology	IMAGE PLATE
Detector	RIGAKU IMAGE PLATE
Spacegroup name	P 1
Unit cell lengths	52.020, 64.230, 70.670
Unit cell angles	70.58, 72.81, 73.84

Refinement procedure

Resolution	19.800 - 2.000
Rwork	0.152
R-free	0.01940 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pnk
RMSD bond length	0.013
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	Agrovata
Phasing software	AMoRE
Refinement software	REFMAC (5.0.36)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.800 *	2.430
High resolution limit [Å]	2.000	2.000
Rmerge	0.040	0.101
Total number of observations	102704 *
Number of reflections	50677
<I/σ(I)>	14.8	7.1
Completeness [%]	93.0	80
Redundancy	2	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.2		50MM MOPS PH 7.2, 12% MME PEG2K, STREAK-SEEDING

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11 (mg/ml)
2	1	drop	PEG2000 MME	11 (%(w/v))
3	1	drop	MOPS	50 (mM)	pH7.2