2AE0

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	4.2	280	PEG 8000, sodium chloride, sodium acetate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 280K

Crystal Properties
Matthews coefficient	Solvent content
4.47	72.47

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 103.873	�� = 90
b = 103.873	�� = 90
c = 109.777	�� = 120

Symmetry
Space Group	P 31 2 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	ADSC QUANTUM 4		2002-09-23	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID14-1	0.934, 0.9794, 0.9792, 0.9393	ESRF	ID14-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	2	30	100	0.049			46854	46854		2

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2	2.07	100	100	0.501

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MAD	THROUGHOUT	2	30	46854	46646	2388	99.98	0.205	0.205	0.203	0.237	RANDOM	37.227

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
2.7	1.35		2.7		-4.04

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	7.786
r_scbond_it	5.261
r_mcangle_it	3.165
r_mcbond_it	2.051
r_dihedral_angle_1_deg	1.406
r_angle_refined_deg	1.124
r_nbd_refined	0.18
r_symmetry_vdw_refined	0.176
r_xyhbond_nbd_refined	0.13
r_chiral_restr	0.102

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	7.786
r_scbond_it	5.261
r_mcangle_it	3.165
r_mcbond_it	2.051
r_dihedral_angle_1_deg	1.406
r_angle_refined_deg	1.124
r_nbd_refined	0.18
r_symmetry_vdw_refined	0.176
r_xyhbond_nbd_refined	0.13
r_chiral_restr	0.102
r_symmetry_hbond_refined	0.081
r_bond_refined_d	0.004
r_gen_planes_refined	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2637
Nucleic Acid Atoms
Solvent Atoms	278
Heterogen Atoms	8

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
SnB	phasing
SOLVE	phasing
RESOLVE	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.