SitesBLAST
Comparing Synpcc7942_0171 FitnessBrowser__SynE:Synpcc7942_0171 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
41% identity, 87% coverage: 43:365/372 of query aligns to 30:352/486 of 4pcuA
- active site: K77 (= K88), S105 (≠ A116), D237 (= D249), S305 (= S318)
- binding protoporphyrin ix containing fe: A182 (≠ L194), P185 (≠ R197), L186 (≠ Q198), Y189 (= Y201), R222 (≠ L234), T269 (≠ A282)
- binding pyridoxal-5'-phosphate: K77 (= K88), N107 (= N118), G212 (= G224), T213 (= T225), G214 (= G226), T216 (= T228), G261 (= G274), S305 (= S318), P331 (≠ C344), D332 (= D345)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
41% identity, 87% coverage: 43:365/372 of query aligns to 72:396/551 of P35520
- P78 (≠ N49) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- G85 (= G56) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T58) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (vs. gap) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (vs. gap) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
- C109 (≠ A78) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P83) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
- K119 (= K88) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ F94) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
- M126 (≠ I95) to V: in CBSD; loss of activity
- E131 (= E100) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G108) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V112) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E113) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G117) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N118) binding
- L154 (= L123) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A124) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- C165 (= C134) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
- M173 (≠ Q142) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
- E176 (= E145) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
- V180 (≠ L149) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T159) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A179) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ L194) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N196) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
- A231 (= A199) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ A202) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
- GTGGT 256:260 (= GTGGT 224:228) binding
- T257 (= T225) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A230) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
- R266 (≠ L234) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K237) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S240) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V243) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
- I278 (≠ V246) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
- D281 (= D249) to N: in CBSD; loss of activity
- A288 (≠ Y256) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ S270) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
- G305 (= G274) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G276) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
- V320 (≠ I289) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D290) to V: in CBSD; loss of activity
- R336 (≠ Y305) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
- L338 (= L307) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- G347 (= G316) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S318) binding ; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- T353 (≠ N322) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T338) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D345) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ A348) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
- K384 (≠ R353) to E: in CBSD; severe form; dbSNP:rs121964967
Sites not aligning to the query:
- 18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
- 49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
- 52 binding axial binding residue
- 58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
- 65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
- 69 A → P: in dbSNP:rs17849313
- 422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- 427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- 435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- 439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- 444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- 449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- 466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- 500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- 526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
- 539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- 540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
41% identity, 85% coverage: 51:365/372 of query aligns to 40:356/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ L194), P189 (≠ R197), L190 (≠ Q198), Y193 (= Y201), R226 (≠ L234)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K88), T106 (= T115), S107 (≠ A116), N109 (= N118), T110 (= T119), Q182 (= Q190), G216 (= G224), T217 (= T225), G218 (= G226), T220 (= T228), G265 (= G274), S309 (= S318), P335 (≠ C344), D336 (= D345)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
41% identity, 85% coverage: 51:365/372 of query aligns to 40:356/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ L194), P189 (≠ R197), L190 (≠ Q198), Y193 (= Y201), R226 (≠ L234)
- binding pyridoxal-5'-phosphate: K79 (= K88), N109 (= N118), G216 (= G224), T217 (= T225), G218 (= G226), T220 (= T228), G265 (= G274), S309 (= S318), P335 (≠ C344), D336 (= D345)
Sites not aligning to the query:
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 86% coverage: 45:365/372 of query aligns to 1:316/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
44% identity, 84% coverage: 53:365/372 of query aligns to 7:314/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
44% identity, 84% coverage: 53:365/372 of query aligns to 7:314/458 of 7xnzB
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
37% identity, 86% coverage: 47:365/372 of query aligns to 8:329/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
37% identity, 86% coverage: 47:365/372 of query aligns to 8:329/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K88), T82 (= T119), Q154 (= Q190), G188 (= G224), T189 (= T225), G190 (= G226), T192 (= T228), G238 (= G274), I239 (= I275), Y241 (≠ N277), S282 (= S318), P308 (≠ C344), D309 (= D345)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
37% identity, 87% coverage: 41:365/372 of query aligns to 1:336/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ T215)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K88), T78 (= T115), S79 (≠ A116), N81 (= N118), T82 (= T119), Q154 (= Q190), A192 (≠ T223), G193 (= G224), T194 (= T225), G195 (= G226), T197 (= T228), G242 (= G274), S286 (= S318), P315 (≠ C344), D316 (= D345)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
37% identity, 87% coverage: 41:365/372 of query aligns to 1:336/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ T215)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K88), T78 (= T115), S79 (≠ A116), N81 (= N118), T82 (= T119), Q154 (= Q190), A192 (≠ T223), G193 (= G224), T194 (= T225), G195 (= G226), T197 (= T228), G242 (= G274), Y245 (≠ N277), S286 (= S318), P315 (≠ C344), D316 (= D345)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
37% identity, 87% coverage: 41:365/372 of query aligns to 1:336/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ T215)
- binding pyridoxal-5'-phosphate: K50 (= K88), N81 (= N118), A192 (≠ T223), G193 (= G224), T194 (= T225), G195 (= G226), T197 (= T228), G242 (= G274), S286 (= S318), P315 (≠ C344), D316 (= D345)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
40% identity, 87% coverage: 47:368/372 of query aligns to 31:350/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ L194), P184 (≠ R197), Y188 (= Y201), R221 (≠ L234)
- binding pyridoxal-5'-phosphate: K74 (= K88), N104 (= N118), G209 (≠ A222), G211 (= G224), T212 (= T225), G213 (= G226), G214 (= G227), T215 (= T228), G256 (= G274), S300 (= S318), P326 (≠ C344), D327 (= D345)
Sites not aligning to the query:
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
38% identity, 87% coverage: 42:365/372 of query aligns to 1:335/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G214), N183 (≠ T215)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K88), N80 (= N118), A191 (≠ T223), G192 (= G224), T193 (= T225), G194 (= G226), T196 (= T228), G241 (= G274), S285 (= S318), P314 (≠ C344), D315 (= D345)
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
41% identity, 84% coverage: 55:368/372 of query aligns to 43:357/504 of Q2V0C9
- K78 (= K88) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N118) binding
- GTGGT 215:219 (= GTGGT 224:228) binding
- S307 (= S318) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
38% identity, 87% coverage: 44:368/372 of query aligns to 34:360/500 of 3pc2A
- active site: K80 (= K88), S310 (= S318)
- binding protoporphyrin ix containing fe: A187 (≠ L194), P190 (≠ R197), L191 (≠ Q198), Y194 (= Y201), R227 (≠ L234)
- binding pyridoxal-5'-phosphate: K80 (= K88), N110 (= N118), A216 (≠ T223), G217 (= G224), T218 (= T225), A219 (≠ G226), T221 (= T228), G266 (= G274), S310 (= S318), P336 (≠ C344), D337 (= D345)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
38% identity, 87% coverage: 44:368/372 of query aligns to 36:362/504 of 3pc4A
- active site: K82 (= K88), S312 (= S318)
- binding protoporphyrin ix containing fe: A189 (≠ L194), P192 (≠ R197), L193 (≠ Q198), Y196 (= Y201), R229 (≠ L234), T276 (≠ A282)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K88), T109 (= T115), S110 (≠ A116), N112 (= N118), T113 (= T119), Q185 (= Q190), A218 (≠ T223), G219 (= G224), T220 (= T225), A221 (≠ G226), T223 (= T228), G268 (= G274), I269 (= I275), Y271 (≠ N277), S312 (= S318), P338 (≠ C344), D339 (= D345)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
38% identity, 87% coverage: 44:368/372 of query aligns to 36:362/504 of 3pc3A
- active site: K82 (= K88), S312 (= S318)
- binding protoporphyrin ix containing fe: A189 (≠ L194), P192 (≠ R197), L193 (≠ Q198), Y196 (= Y201), R229 (≠ L234)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K88), T109 (= T115), S110 (≠ A116), N112 (= N118), T113 (= T119), Q185 (= Q190), A218 (≠ T223), G219 (= G224), T220 (= T225), A221 (≠ G226), T223 (= T228), G268 (= G274), I269 (= I275), S312 (= S318), P338 (≠ C344), D339 (= D345)
Sites not aligning to the query:
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
41% identity, 80% coverage: 54:352/372 of query aligns to 6:297/302 of 2efyA
- active site: K40 (= K88), S70 (≠ A116), E200 (≠ D249), S204 (= S253), S263 (= S318)
- binding 5-oxohexanoic acid: T69 (= T115), G71 (= G117), T73 (= T119), Q141 (= Q190), G175 (= G224), G219 (= G274), M220 (≠ I275), P222 (≠ N277)
- binding pyridoxal-5'-phosphate: K40 (= K88), N72 (= N118), Y172 (≠ A221), G175 (= G224), T176 (= T225), G177 (= G226), T179 (= T228), G219 (= G274), S263 (= S318), P289 (≠ C344), D290 (= D345)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
41% identity, 80% coverage: 54:352/372 of query aligns to 6:297/302 of 2ecqA
- active site: K40 (= K88), S70 (≠ A116), E200 (≠ D249), S204 (= S253), S263 (= S318)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K88), G71 (= G117), T73 (= T119), Q141 (= Q190), G219 (= G274)
- binding pyridoxal-5'-phosphate: K40 (= K88), N72 (= N118), Y172 (≠ A221), G173 (≠ A222), G175 (= G224), T176 (= T225), T179 (= T228), G219 (= G274), S263 (= S318), P289 (≠ C344)
Query Sequence
>Synpcc7942_0171 FitnessBrowser__SynE:Synpcc7942_0171
MAARDIHFANRDRRPSPLVGAFLLRVREPKQVGRIKPGCPTEKRMDIRNGFIDTIGNTPL
IRLNSLSEATGCNILGKAEFLNPGGSVKDRAALFIIEDAERQGKLRPGGTVVEGTAGNTG
IGLAHICNAKGYRCLIVIPETQSQEKIDLLRTLGAEVRTVPAVPYRDPNNYVKVSGRLAE
ELDNAIWANQFDNLANRQAHYATTGPEIWQQTEGTVDAWVAATGTGGTYAGVALYLKEQS
SKVRCVVADPMGSGLYSWVKTGEIHLEGSSVTEGIGNSRITANMQDVPIDDAIQIADPEA
LEIIYQLLHRDGLFMGGSVGINVAAAYRLAKEMGPGHTIVTVLCDGGARYQSRLFNAEWL
ASKGLQMPQVTT
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory