5VPU

Crystal Structure of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase bound to 3-phosphoglycerate, from Acinetobacter baumannii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2017-04-29
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	P 1 21 1
Unit cell lengths	45.940, 82.090, 72.410
Unit cell angles	90.00, 97.64, 90.00

Refinement procedure

Resolution	41.045 - 1.500
R-factor	0.1355
Rwork	0.135
R-free	0.16400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1o98
RMSD bond length	0.006
RMSD bond angle	1.108
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	41.045	41.045	1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.048	0.034	0.151
Rmeas	0.052	0.037	0.169
Total number of observations	517771
Number of reflections	84305	986	6026
<I/σ(I)>	22.98	38.03	9.05
Completeness [%]	99.0	99.4	95.5
Redundancy	6.142	6.508	5.148
CC(1/2)	0.999	0.999	0.987

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	MCSG1 F2: 0.2 M Ammonium Acetate 0.1 M Bis-Tris: HCl, pH 6.5 25 % (w/v) PEG 3350 +3mM 3-phosphoglycerate cryo:15% Ethylene glycol PS38071 24.7mg/mL, 0.4+0.4 puck frn7-12