3MOA

Crystal structure of the neutralizing HIV antibody 2F5 Fab fragment (recombinantly produced Fab) with 17 aa gp41 MPER-derived peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	58.820, 65.229, 174.205
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.683 - 2.300
R-factor	0.1862
Rwork	0.184
R-free	0.21930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tji
RMSD bond length	0.027
RMSD bond angle	1.348
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	PHENIX
Refinement software	PHENIX ((phenix.refine: dev_271))

Data quality characteristics

	Overall
Low resolution limit [Å]	43.700
High resolution limit [Å]	2.300
Rmerge	0.062
Number of reflections	30678
<I/σ(I)>	15.4
Completeness [%]	100.0
Redundancy	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	5.6	298	Reservoir; Hampton Research Crystal Screen 40 = 20% isopropanol, 20% PEG 4000, 100 mM Na citrate pH 5.6. Drop: 0.5 uL protein + 0.35 uL reservoir. Reservoir was NOT supplemented with 100 mM NaCl as in Ofek et al. 2004., VAPOR DIFFUSION, temperature 298K