Is single-wavelength anomalous scattering sufficient for solving phases? A comparison of different methods for a 2.1 A structure solution.
The structure of rusticyanin is the largest unknown structure (M(r) = 16.8 kDa) which has been recently solved by the direct-methods approach using only single-wavelength anomalous scattering (SAS) data from the native protein [Harvey et al. (1998). Acta Cryst. D54, 629-635]. Here, the results of the Sim distribution approach [Hendrickson & Teeter (1981). Nature (London), 290, 107-113] and of the CCP4 procedure MLPHARE [Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763] are compared with those from direct methods. Analysis against the final refined model shows that direct methods produced significantly better phases (average phase error 56 degrees ) and therefore significantly better electron-density maps than the Sim distribution and MLPHARE approaches (average phase error was around 63 degrees in both cases).
Yu-dong
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L
Institute of Physics, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
Harvey
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I
Yuan-xin
G
G
Chao-de
Z
Z
Yi-zong
H
H
Hai-fu
F
F
Hasnain
S S
SS
Hao
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Q
D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray / Q000379:methods; D008432:Mathematical Computing; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions
D001426:Bacterial Proteins; D012996:Solutions; C012543:rusticyanin; D001400:Azurin