1FXV

PENICILLIN ACYLASE MUTANT IMPAIRED IN CATALYSIS WITH PENICILLIN G IN THE ACTIVE SITE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-10-07
Detector	MACSCIENCE
Spacegroup name	P 1
Unit cell lengths	50.930, 63.966, 64.189
Unit cell angles	72.85, 73.77, 74.06

Refinement procedure

Resolution	20.000 - 2.250
Rwork	0.187
R-free	0.23600
RMSD bond length	0.005
RMSD bond angle	0.730 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.290
High resolution limit [Å]	2.250	2.250
Rmerge	0.068	0.188
Number of reflections	32525
<I/σ(I)>	11.8
Completeness [%]	94.3	79.9
Redundancy	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	4 *	drop consists of equal amounts of protein and precipitant solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	8 (mg/ml)
2	1	reservoir	mPEG2000	12-15 (%)	precipitant
3	1	reservoir	MOPS	50 (mM)	precipitant