1BHY

LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF P64K FROM MASC DATA

Summary for 1BHY

• Entry DOI: 10.2210/pdb1bhy/pdb
• Descriptor: P64K, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total)
• Functional Keywords: outer membrane protein, masc, multiwavelength anomalous solvent contrast
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 51583.54

Authors

Ramin, M.,Shepard, W.,Fourme, R.,Kahn, R. (deposition date: 1998-06-10, release date: 1998-11-04, Last modification date: 2024-12-25)

Primary citation

Ramin, M.,Shepard, W.,Fourme, R.,Kahn, R.
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.
Acta Crystallogr.,Sect.D, 55:157-167, 1999

PubMed Abstract: A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d >/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.

PubMed: 10089406
DOI: 10.1107/S090744499800626X

Experimental method

X-RAY DIFFRACTION (4.18 Å)