3PVA

PENICILLIN V ACYLASE FROM B. SPHAERICUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	120
Spacegroup name	P 1
Unit cell lengths	47.400, 129.600, 156.700
Unit cell angles	88.30, 83.40, 84.60

Refinement procedure

Resolution	14.000 - 2.800
R-factor	0.211 *
Rwork	0.211
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	REFINED STRUCTURE FROM HEXAGONAL FORM
RMSD bond length	0.020
RMSD bond angle	0.040
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall
Low resolution limit [Å]	18.000
High resolution limit [Å]	2.800
Rmerge	0.053
Total number of observations	111412 *
Number of reflections	77056
<I/σ(I)>	11.2
Completeness [%]	85.0
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.4		5MM DTT, 30% AS, 1% SUCROSE, 0.2M NA PHOSPHATE, PH 6.4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium phosphate	0.1 (M)	pH6.4
2	1	reservoir	dithiothreitol	3 (mM)
3	1	reservoir	ammonium sulfate
4	1	reservoir	sucrose solution	0.9 (%(w/v))
5	1	drop	protain	15 (mg/ml)
6	1	drop	sodium phosphate	0.2 (M)