9PUF

Crystal Structure of N-Phenylalanine Peptoid-modified Collagen Triple Helix (GPX)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-10-04
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	C 1 2 1
Unit cell lengths	113.541, 24.081, 15.029
Unit cell angles	90.00, 94.50, 90.00

Refinement procedure

Resolution	56.595 - 1.297
R-factor	0.1495
Rwork	0.147
R-free	0.16820
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	collagen peptide
Data reduction software	XDS (Feb 5, 2021)
Data scaling software	Aimless (0.5.32)
Phasing software	PHASER
Refinement software	PHENIX (1.16_3549)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	56.600	56.600	1.320
High resolution limit [Å]	1.290	7.090	1.290
Rmerge	0.151	0.062	0.653
Rmeas	0.158	0.064	0.684
Rpim	0.044	0.018	0.200
Total number of observations	128471	812	4551
Number of reflections	10169	72	418
<I/σ(I)>	11.6	22.8	2.9
Completeness [%]	98.9	99.1	85.6
Redundancy	12.6	11.3	10.9
CC(1/2)	0.998	1.000	0.877

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	294	protein in water at 5 mg/ml mixed 50:50 with 40% (v/v) PEG 600, 100 mM Imidazole/Hydrochloric acid pH8.0, 200 mM Zinc acetate