5VMB

Crystal structure of a glycine hydroxymethyltransferase from Acinetobacter baumannii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-03-04
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 64
Unit cell lengths	95.840, 95.840, 109.690
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.815 - 2.500
R-factor	0.1867
Rwork	0.181
R-free	0.23320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p3m
RMSD bond length	0.007
RMSD bond angle	0.874
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	38.815	38.815	2.570
High resolution limit [Å]	2.500	11.180	2.500
Rmerge	0.037	0.018	0.593
Rmeas	0.040	0.021	0.657
Number of reflections	19797	193	1466
<I/σ(I)>	25.88	56.42	2.57
Completeness [%]	99.6	79.8	100
Redundancy	5.492	4.047	5.514
CC(1/2)	1.000	0.999	0.849

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		289	AcbaC.00008.a.B1.PW37629 at 18.5 mg/mL with 3 mM glycine, 3 mM ADP, 2 mM MgCl2 against Morpheus screen condition E5 10% PEG 10,000, 20% PEG 550 MME, 30 mM each diethyleneglycol, triethyleneglycol, tetraethyleneglycol, pentaethyleneglycol, 0.1 M MOPS/Hepes pH 7.5, crystal tracking ID 261070e5, unique puck ID eob8-7