1IU8

The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-18B
Synchrotron site	Photon Factory
Beamline	BL-18B
Temperature [K]	100
Detector technology	CCD
Collection date	2001-06-23
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	C 1 2 1
Unit cell lengths	104.899, 66.479, 76.396
Unit cell angles	90.00, 128.68, 90.00

Refinement procedure

Resolution	20.000 - 1.600
R-factor	0.189 *
Rwork	0.189
R-free	0.21400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iof
RMSD bond length	0.004
RMSD bond angle	22.920 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.600	1.686
High resolution limit [Å]	1.600	1.600
Rmerge	0.061 *	0.269 *
Total number of observations	207328 *
Number of reflections	54101
<I/σ(I)>	8	3
Completeness [%]	100.0	100
Redundancy	3.8	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	4 *	MPD, Magnesium Chlolide, Imidazole, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	imidazole	100 (mM)	pH7.4-9.0
2	1	reservoir	MPD	35-38 (%)
3	1	reservoir		0.1-0.2 (M)
4	1	drop	protein	10 (mg/ml)