1X10

Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192A) from a Hyperthermophile, Pyrococcus furiosus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL40B2
Synchrotron site	SPring-8
Beamline	BL40B2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-12-15
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	47.440, 103.961, 187.494
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
Rwork	0.227
R-free	0.24810
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ioi
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.048	0.083
Number of reflections	62100
<I/σ(I)>	33	15.2
Completeness [%]	96.4	86
Redundancy	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	PEG4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K