9SD1

The R62Q clinical variant of human bisphosphoglycerate mutase (hBPGM).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-07-03
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.9677
Spacegroup name	P 1
Unit cell lengths	37.550, 47.242, 143.043
Unit cell angles	86.86, 84.12, 83.17

Refinement procedure

Resolution	71.080 - 2.500
R-factor	0.2107
Rwork	0.208
R-free	0.26360
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.542
Data reduction software	xia2
Data scaling software	Aimless (0.7.4)
Phasing software	MOLREP (11.9.02)
Refinement software	PHENIX ((1.21.2_5419: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	71.080	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.194	0.757
Rmeas	0.247	0.966
Rpim	0.151	0.591
Total number of observations	84866	9455
Number of reflections	31472	3531
<I/σ(I)>	3.2	1.1
Completeness [%]	93.9
Redundancy	2.7	2.7
CC(1/2)	0.951	0.513

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	0.09 M NPS (0.3M Sodium Nitrate, 0.3 Sodium Phosphate dibasic, 0.3M Ammonium Sulfate), 0.1 M of Buffer System2 (Sodium HEPES; MOPS (acid)) pH 7.5, 30 % v/v of Precipitant Mix 1 (40% v/v PEG 500* MME; 20 % w/v PEG 20000)