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
Hauptverfasser: Fujita, Junso, Miyazaki, Yuma, Hirose, Mika, Nagao, Chioko, Mizohata, Eiichi, Matsumoto, Yoshimi, Mizuguchi, Kenji, Inoue, Tsuyoshi, Matsumura, Hiroyoshi
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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.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309113017727