Knowledge (XXG)

Difference density map

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Difference density maps are usually calculated using Fourier coefficients which are the differences between the observed structure factor amplitudes from the X-ray diffraction experiment and the calculated structure factor amplitudes from the current model, using the phase from the model for both
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The use of ML weighting reduces model bias (due to using the model's phase) in the 2 Fo–Fc map, which is the main estimate of the true density. However, it does not fully eliminate such bias.
412:" scale factor. These coefficients are derived from the gradient of the likelihood function of the observed structure factors on the basis of the current model. A difference map built with 47:
with positive density—electron density where there's nothing in the model, usually corresponding to some constituent of the crystal that hasn't been modelled, for example a
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It is now normal to also include maximum-likelihood weighting terms which take into account the estimated errors in the current model:
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terms (since no phases are available for the observed data). The two sets of structure factors must be on the same scale.
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Terwilliger, TC; Grosse-Kunstleve, RW; Afonine, PV; Moriarty, NW; Adams, PD; Read, RJ; Zwart, PH; Hung, LW (May 2008).
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or that it is modelled in the wrong place—in red. The typical contouring (display threshold) is set at 3σ.
655: 52: 578:"Iterative-build OMIT maps: map improvement by iterative model building and refinement without model bias" 17: 589: 478: 615: 558: 506: 605: 597: 548: 540: 496: 486: 56: 29: 636: 465:
Yamashita, Keitaro; Palmer, Colin M.; Burnley, Tom; Murshudov, Garib N. (1 October 2021).
401: 593: 482: 610: 577: 553: 528: 501: 466: 649: 467:"Cryo-EM single-particle structure refinement and map calculation using Servalcat" 544: 640: 601: 491: 44: 619: 562: 510: 386:{\displaystyle C_{diffmap}=(m|F_{obs}|-D|F_{calc}|)exp(2\pi i\phi _{calc})} 441: 219:{\displaystyle C_{diffmap}=(|F_{obs}|-|F_{calc}|)exp(2\pi i\phi _{calc})} 32:
of the crystal and the electron density explained by the current model.
529:"You are lost without a map: Navigating the sea of protein structures" 28:
shows the spatial distribution of the difference between the measured
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which is an estimate of the cosine of the error in the phase, and
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Acta Crystallographica. Section D, Biological Crystallography
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Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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A way to compute this map has been formulated for cyro-EM.
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Acta Crystallographica Section D Structural Biology
527:Lamb, AL; Kappock, TJ; Silvaggi, NR (April 2015). 385: 218: 522: 520: 8: 609: 552: 500: 490: 365: 332: 317: 308: 297: 285: 276: 243: 237: 198: 165: 150: 141: 133: 121: 112: 82: 76: 442:"RCSB PDB: X-ray Electron Density Maps" 432: 43:Conventionally, they are displayed as 7: 14: 380: 349: 337: 333: 309: 298: 277: 270: 213: 182: 170: 166: 142: 134: 113: 109: 1: 420:is known as a mFo – DFc map. 545:10.1016/j.bbapap.2014.12.021 672: 602:10.1107/S0907444908004319 492:10.1107/S2059798321009475 440:Bank, RCSB Protein Data. 53:crystallisation adjutant 387: 220: 22:difference density map 637:Electron density maps 388: 221: 18:X-ray crystallography 236: 75: 594:2008AcCrD..64..515T 483:2021AcCrD..77.1282Y 383: 216: 477:(10): 1282–1291. 663: 624: 623: 613: 588:(Pt 5): 515–24. 573: 567: 566: 556: 524: 515: 514: 504: 494: 462: 456: 455: 453: 452: 437: 392: 390: 389: 384: 379: 378: 336: 331: 330: 312: 301: 296: 295: 280: 266: 265: 225: 223: 222: 217: 212: 211: 169: 164: 163: 145: 137: 132: 131: 116: 105: 104: 57:radiation damage 30:electron density 671: 670: 666: 665: 664: 662: 661: 660: 656:Crystallography 646: 645: 633: 631:Further reading 628: 627: 575: 574: 570: 526: 525: 518: 464: 463: 459: 450: 448: 439: 438: 434: 429: 411: 402:figure of merit 361: 313: 281: 239: 234: 233: 194: 146: 117: 78: 73: 72: 65: 41: 12: 11: 5: 669: 667: 659: 658: 648: 647: 644: 643: 632: 629: 626: 625: 568: 516: 457: 431: 430: 428: 425: 409: 394: 393: 382: 377: 374: 371: 368: 364: 360: 357: 354: 351: 348: 345: 342: 339: 335: 329: 326: 323: 320: 316: 311: 307: 304: 300: 294: 291: 288: 284: 279: 275: 272: 269: 264: 261: 258: 255: 252: 249: 246: 242: 227: 226: 215: 210: 207: 204: 201: 197: 193: 190: 187: 184: 181: 178: 175: 172: 168: 162: 159: 156: 153: 149: 144: 140: 136: 130: 127: 124: 120: 115: 111: 108: 103: 100: 97: 94: 91: 88: 85: 81: 64: 61: 40: 37: 13: 10: 9: 6: 4: 3: 2: 668: 657: 654: 653: 651: 642: 638: 635: 634: 630: 621: 617: 612: 607: 603: 599: 595: 591: 587: 583: 579: 572: 569: 564: 560: 555: 550: 546: 542: 539:(4): 258–68. 538: 534: 530: 523: 521: 517: 512: 508: 503: 498: 493: 488: 484: 480: 476: 472: 468: 461: 458: 447: 443: 436: 433: 426: 424: 421: 419: 415: 407: 403: 399: 375: 372: 369: 366: 362: 358: 355: 352: 346: 343: 340: 327: 324: 321: 318: 314: 305: 302: 292: 289: 286: 282: 273: 267: 262: 259: 256: 253: 250: 247: 244: 240: 232: 231: 230: 208: 205: 202: 199: 195: 191: 188: 185: 179: 176: 173: 160: 157: 154: 151: 147: 138: 128: 125: 122: 118: 106: 101: 98: 95: 92: 89: 86: 83: 79: 71: 70: 69: 62: 60: 58: 54: 50: 46: 38: 36: 33: 31: 27: 23: 19: 585: 581: 571: 536: 532: 474: 470: 460: 449:. Retrieved 446:www.rcsb.org 445: 435: 422: 417: 413: 408:is a "σ 405: 397: 395: 228: 66: 42: 34: 25: 21: 15: 641:Proteopedia 63:Calculation 45:isosurfaces 451:2021-01-08 427:References 363:ϕ 356:π 303:− 196:ϕ 189:π 139:− 26:Fo–Fc map 650:Category 620:18453687 563:25554228 511:34605431 611:2424225 590:Bibcode 554:5051661 502:8489229 479:Bibcode 39:Display 618:  608:  561:  551:  509:  499:  396:where 49:ligand 400:is a 51:or a 616:PMID 559:PMID 537:1854 507:PMID 416:and 20:, a 639:on 606:PMC 598:doi 549:PMC 541:doi 497:PMC 487:doi 24:or 16:In 652:: 614:. 604:. 596:. 586:64 584:. 580:. 557:. 547:. 535:. 531:. 519:^ 505:. 495:. 485:. 475:77 473:. 469:. 444:. 622:. 600:: 592:: 565:. 543:: 513:. 489:: 481:: 454:. 418:D 414:m 410:A 406:D 398:m 381:) 376:c 373:l 370:a 367:c 359:i 353:2 350:( 347:p 344:x 341:e 338:) 334:| 328:c 325:l 322:a 319:c 315:F 310:| 306:D 299:| 293:s 290:b 287:o 283:F 278:| 274:m 271:( 268:= 263:p 260:a 257:m 254:f 251:f 248:i 245:d 241:C 214:) 209:c 206:l 203:a 200:c 192:i 186:2 183:( 180:p 177:x 174:e 171:) 167:| 161:c 158:l 155:a 152:c 148:F 143:| 135:| 129:s 126:b 123:o 119:F 114:| 110:( 107:= 102:p 99:a 96:m 93:f 90:f 87:i 84:d 80:C

Index

X-ray crystallography
electron density
isosurfaces
ligand
crystallisation adjutant
radiation damage
figure of merit
"RCSB PDB: X-ray Electron Density Maps"
"Cryo-EM single-particle structure refinement and map calculation using Servalcat"
Bibcode
2021AcCrD..77.1282Y
doi
10.1107/S2059798321009475
PMC
8489229
PMID
34605431


"You are lost without a map: Navigating the sea of protein structures"
doi
10.1016/j.bbapap.2014.12.021
PMC
5051661
PMID
25554228
"Iterative-build OMIT maps: map improvement by iterative model building and refinement without model bias"
Bibcode
2008AcCrD..64..515T
doi

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