Expression, purification, crystallization and preliminary crystallographic study of FtsA from methicillin-resistant Staphylococcus aureus
FtsA from methicillin‐resistant Staphylococcus aureus (MRSA) was cloned, overexpressed and purified. The protein was crystallized using the sitting‐drop vapour‐diffusion technique. A cocrystal with β‐γ‐imidoadenosine 5′‐phosphate (AMPPNP; a nonhydrolysable ATP analogue) was grown using PEG 3350 as a...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2013-08, Vol.69 (8), p.895-898 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | FtsA from methicillin‐resistant Staphylococcus aureus (MRSA) was cloned, overexpressed and purified. The protein was crystallized using the sitting‐drop vapour‐diffusion technique. A cocrystal with β‐γ‐imidoadenosine 5′‐phosphate (AMPPNP; a nonhydrolysable ATP analogue) was grown using PEG 3350 as a precipitant at 293 K. X‐ray diffraction data were collected to a resolution of 2.3 Å at 100 K. The crystal belonged to the monoclinic space group P21, with unit‐cell parameters a = 75.31, b = 102.78, c = 105.90 Å, β = 96.54°. The calculated Matthews coefficient suggested that the asymmetric unit contained three or four monomers. |
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ISSN: | 1744-3091 1744-3091 2053-230X |
DOI: | 10.1107/S1744309113017727 |