7KNG

2.10A resolution structure of independent Phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Ce-2 Y7F)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-02-15
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	1.00000
Spacegroup name	P 1 2 1
Unit cell lengths	73.862, 75.471, 101.360
Unit cell angles	90.00, 99.11, 90.00

Refinement procedure

Resolution	44.690 - 2.100
R-factor	0.1693
Rwork	0.167
R-free	0.21980
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5kgn
Data reduction software	XDS
Data scaling software	Aimless (0.7.4)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.18rc1_3769)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	44.690	44.690	2.150
High resolution limit [Å]	2.100	9.620	2.100
Rmerge	0.105	0.030	0.581
Total number of observations	219493	2317	15460
Number of reflections	64166	694	4496
<I/σ(I)>	8.9	27.6	2.1
Completeness [%]	99.7	96.8	99.9
Redundancy	3.4	3.3	3.4
CC(1/2)	0.995	0.998	0.783

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	25% (w/v) PEG 3350, 0.1 M Hepes, 3% (w/v) Trimethylamine N-oxide