1V7H

Crystal Structures of Collagen Model Peptides with Pro-Hyp-Gly Sequence at 1.26 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44XU
Synchrotron site	SPring-8
Beamline	BL44XU
Temperature [K]	100
Detector technology	CCD
Collection date	2002-06-11
Detector	OXFORD PX210
Wavelength(s)	0.9
Spacegroup name	P 1 21 1
Unit cell lengths	13.892, 26.115, 19.954
Unit cell angles	90.00, 105.95, 90.00

Refinement procedure

Resolution	10.000 - 1.250
Rwork	0.127
R-free	0.18280
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	(PRO-HYP-GLY)10 structure reported in V.NAGARAJAN S.KAMITORI K.OKUYAMA J.BIOCHEM. 125 310 (1999).
RMSD bond length	0.016
RMSD bond angle	0.026
Data reduction software	CrystalClear
Data scaling software	CrystalClear ((MSC/RIGAKU))
Phasing software	SHELXS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.280
High resolution limit [Å]	1.240	1.240
Rmerge	0.042	0.057
Number of reflections	3257
<I/σ(I)>		8.2
Completeness [%]		74

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		283	PEG200, ACETIC ACID, VAPOR DIFFUSION, HANGING DROP, temperature 283K