7TL7

1.90A resolution structure of independent phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Sa-D2)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-10-31
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.00000
Spacegroup name	P 1 21 1
Unit cell lengths	77.999, 87.624, 151.341
Unit cell angles	90.00, 97.13, 90.00

Refinement procedure

Resolution	39.840 - 1.900
R-factor	0.1733
Rwork	0.171
R-free	0.21570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5kgn
Data reduction software	XDS
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER
Refinement software	PHENIX (1.20rc2_4402)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.120	48.120	1.930
High resolution limit [Å]	1.900	10.410	1.900
Rmerge	0.081	0.030	0.768
Total number of observations	547906	3497	27523
Number of reflections	158753	1026	7783
<I/σ(I)>	9.8	27	1.6
Completeness [%]	99.7	98.4	99.9
Redundancy	3.5	3.4	3.5
CC(1/2)	0.997	0.998	0.655

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	MORPHEUS Screen Condition H4: 37.5% (w/v) of precipitant mix 4: (25% (v/v) MPD: 25% (w/v) PEG 1000: 25% (w/v) PEG 3350), 100 mM of MB1: (1.0 M imidazole, MES), 100 mM of MAA: (0.2 M DL-Glutamic acid monohydrate: 0.2 M DL-Alanine: 0.2M Glycine: 0.2 M DL-Lysine monohydrochloride: 0.2 M DL-Serine