Assessing the prospect of XAFS experiments of metalloproteins under in vivo conditions at Indus-2 synchrotron facility, India

被引:0
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作者
Lahiri, Debdutta [1 ]
Agrawal, Richa [2 ]
Chandravanshi, Khileshwari [3 ]
Rajput, Parasmani [3 ]
Agrawal, Ankur [3 ]
Dwivedi, Ashutosh [3 ]
Makde, Ravindra D. [3 ]
Jha, S. N. [3 ]
Garg, Nandini [1 ,4 ]
机构
[1] Bhabha Atom Res Ctr, High Pressure & Synchrotron Radiat Phys, Mumbai 400085, Maharashtra, India
[2] Univ Chicago, Dept Biochem & Mol Biol, 929 E 57th St, Chicago, IL 60637 USA
[3] Bhabha Atom Res Ctr, Beamline Dev & Applicat Sect, Mumbai 400085, Maharashtra, India
[4] Homi Bhabha Natl Inst, Training Sch Complex, Mumbai 400094, Maharashtra, India
关键词
XAFS; metalloproteins; X-RAY-ABSORPTION; PROTEIN CRYSTALLOGRAPHY; STRUCTURAL BIOLOGY; ACTIVE-SITE; ZINC SITES; SPECTROSCOPY; BEAMLINE; EXAFS; BINDING; COORDINATION;
D O I
10.1107/S1600577522011791
中图分类号
TH7 [仪器、仪表];
学科分类号
0804 ; 080401 ; 081102 ;
摘要
The feasibility of X-ray absorption fine-structure (XAFS) experiments of ultradilute metalloproteins under in vivo conditions (T = 300 K, pH = 7) at the BL-9 bending-magnet beamline (Indus-2) is reported, using as an example analogous synthetic Zn (0.1 mM) M1dr solution. The (Zn K-edge) XAFS of M1dr solution was measured with a four-element silicon drift detector. The first-shell fit was tested and found to be robust against statistical noise, generating reliable nearest-neighbor bond results. The results are found to be invariant between physiological and non-physiological conditions, which confirms the robust coordination chemistry of Zn with important biological implications. The scope of improving spectral quality for accommodation of higher-shell analysis is addressed.
引用
收藏
页码:449 / 456
页数:8
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