2XR0

Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	293
Detector technology	CCD
Collection date	2010-04-04
Detector	MARRESEARCH MX-300
Spacegroup name	P 32 2 1
Unit cell lengths	73.500, 73.500, 99.330
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.540 - 2.200
R-factor	0.135
Rwork	0.133
R-free	0.17300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2wyx
RMSD bond length	0.009
RMSD bond angle	1.122
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE: 1.6.4_486))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.540	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.050	0.830
Number of reflections	15962
<I/σ(I)>	31.3	22
Completeness [%]	98.6	97.9
Redundancy	7.5	7.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.5		2.0 A AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PD 5.1. PREPARED IN 99.9% D2O AND MIXED 1:1 WITH PERDEUTERATED PROTEIN PREPARED IN 20 MM NA MES AT PD 6.1 (PH 6.5).