1K5Q

PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PAA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	2000-01-01
Detector	MAC Science DIP-2020
Wavelength(s)	1.5418
Spacegroup name	P 1
Unit cell lengths	50.760, 63.960, 64.240
Unit cell angles	72.86, 73.91, 73.50

Refinement procedure

Resolution	19.000 * - 2.340
R-factor	0.16616
Rwork	0.163
R-free	0.21800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pnk
RMSD bond length	0.020 *
RMSD bond angle	1.251 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.000 *	2.380
High resolution limit [Å]	2.340	2.340
Rmerge	0.043 *	0.098 *
Total number of observations	55158 *
Number of reflections	28382
<I/σ(I)>	15.9	5.5
Completeness [%]	92.9	77.5
Redundancy	1.943

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	4 *	MOPS BUFFER, PEG MME 2K, PAA , pH 7.20, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

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